HCP_DESVH
ID HCP_DESVH Reviewed; 553 AA.
AC P31101;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Hydroxylamine reductase {ECO:0000255|HAMAP-Rule:MF_00069};
DE EC=1.7.99.1 {ECO:0000255|HAMAP-Rule:MF_00069};
DE AltName: Full=Hybrid-cluster protein {ECO:0000255|HAMAP-Rule:MF_00069};
DE Short=HCP {ECO:0000255|HAMAP-Rule:MF_00069};
DE AltName: Full=Prismane protein {ECO:0000255|HAMAP-Rule:MF_00069};
GN Name=hcp {ECO:0000255|HAMAP-Rule:MF_00069}; OrderedLocusNames=DVU_2013;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1339351; DOI=10.1111/j.1432-1033.1992.tb17205.x;
RA Stokkermans J.P.W.G., Pierik A.J., Wolbert R.B.G., Hagen W.R.,
RA van Dongen W.M.A.M., Veeger C.;
RT "The primary structure of a protein containing a putative [6Fe-6S] prismane
RT cluster from Desulfovibrio vulgaris (Hildenborough).";
RL Eur. J. Biochem. 208:435-442(1992).
RN [2]
RP SEQUENCE REVISION TO 202-204.
RA van Dongen W.M.A.M.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [4]
RP PROTEIN SEQUENCE OF 1-14, SUBCELLULAR LOCATION, COFACTOR, AND SUBUNIT.
RX PubMed=1318832; DOI=10.1111/j.1432-1033.1992.tb16976.x;
RA Pierik A.J., Wolbert R.B.G., Mutsaers P.H.A., Hagen W.R., Veeger C.;
RT "Purification and biochemical characterization of a putative [6Fe-6S]
RT prismane-cluster-containing protein from Desulfovibrio vulgaris
RT (Hildenborough).";
RL Eur. J. Biochem. 206:697-704(1992).
RN [5]
RP COFACTOR.
RX PubMed=1318833; DOI=10.1111/j.1432-1033.1992.tb16977.x;
RA Pierik A.J., Hagen W.R., Dunham W.R., Sands R.H.;
RT "Multi-frequency EPR and high-resolution Mossbauer spectroscopy of a
RT putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio
RT vulgaris (Hildenborough). Characterization of a supercluster and superspin
RT model protein.";
RL Eur. J. Biochem. 206:705-719(1992).
RN [6]
RP COFACTOR.
RX PubMed=9492318; DOI=10.1046/j.1432-1327.1998.2510454.x;
RA Kroeckel M., Trautwein A.X., Arendsen A.F., Hagen W.R.;
RT "The prismane protein resolved -- Mossbauer investigation of a 4Fe cluster
RT with an unusual mixture of bridging ligands and metal coordinations.";
RL Eur. J. Biochem. 251:454-461(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER,
RP AND COFACTOR.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RA Arendsen A.F., Hadden J., Card G., McAlpine A.S., Bailey S., Zaitsev V.,
RA Duke E.H.M., Lindley P.F., Kroeckel M., Trautwein A.X., Feiters M.C.,
RA Charnock J.M., Garner C.D., Marritt S.J., Thomson A.J., Kooter I.M.,
RA Johnson M.K., van den Berg W.A.M., van Dongen W.M.A.M., Hagen W.R.;
RT "The 'prismane' protein resolved: X-ray structure at 1.7-A and multiple
RT spectroscopy of two novel 4Fe clusters.";
RL J. Biol. Inorg. Chem. 3:81-95(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER
RP AND IRON-SULFUR-OXYGEN CLUSTER, AND COFACTOR.
RX PubMed=11106482; DOI=10.1021/bi001483m;
RA Cooper S.J., Garner C.D., Hagen W.R., Lindley P.F., Bailey S.;
RT "Hybrid-cluster protein (HCP) from Desulfovibrio vulgaris (Hildenborough)
RT at 1.6 A resolution.";
RL Biochemistry 39:15044-15054(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER
RP AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SULFHYDRATION AT CYS-406, AND
RP SUBUNIT.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=11941509; DOI=10.1007/s00775-001-0326-y;
RA Macedo S., Mitchell E.P., Romao C.V., Cooper S.J., Coelho R., Liu M.Y.,
RA Xavier A.V., LeGall J., Bailey S., Garner C.D., Hagen W.R., Teixeira M.,
RA Carrondo M.A., Lindley P.;
RT "Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774
RT and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A
RT resolution using synchrotron radiation.";
RL J. Biol. Inorg. Chem. 7:514-525(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER
RP AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=12764602; DOI=10.1007/s00775-003-0443-x;
RA Aragao D., Macedo S., Mitchell E.P., Romao C.V., Liu M.Y., Frazao C.,
RA Saraiva L.M., Xavier A.V., LeGall J., van Dongen W.M.A.M., Hagen W.R.,
RA Teixeira M., Carrondo M.A., Lindley P.;
RT "Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans
RT ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at
RT high resolution using synchrotron radiation.";
RL J. Biol. Inorg. Chem. 8:540-548(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER
RP AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=18560155; DOI=10.1107/s0907444908009165;
RA Aragao D., Mitchell E.P., Frazao C.F., Carrondo M.A., Lindley P.F.;
RT "Structural and functional relationships in the hybrid cluster protein
RT family: structure of the anaerobically purified hybrid cluster protein from
RT Desulfovibrio vulgaris at 1.35 A resolution.";
RL Acta Crystallogr. D 64:665-674(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER
RP AND IRON-SULFUR-OXYGEN CLUSTER, AND COFACTOR.
RA Cooper S.J., Garner C.D., Hagen W.R., Lindley P.F., Bailey S.;
RT "Ferricyanide soaked hybrid cluster protein at 1.2A and xenon mapping of
RT the hydrophobic cavity at 1.8A.";
RL Submitted (OCT-2000) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) and
CC H(2)O. {ECO:0000255|HAMAP-Rule:MF_00069}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine;
CC Xref=Rhea:RHEA:22052, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15429, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:28938; EC=1.7.99.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00069};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:11106482, ECO:0000269|PubMed:11941509,
CC ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:1318832,
CC ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12, ECO:0000269|Ref.7};
CC Note=Binds 1 spin-admixed [4Fe-4S] cluster.
CC {ECO:0000269|PubMed:11106482, ECO:0000269|PubMed:11941509,
CC ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:1318832,
CC ECO:0000269|PubMed:18560155};
CC -!- COFACTOR:
CC Name=hybrid [4Fe-2O-2S] cluster; Xref=ChEBI:CHEBI:60519;
CC Evidence={ECO:0000269|PubMed:11106482, ECO:0000269|PubMed:11941509,
CC ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:1318832,
CC ECO:0000269|PubMed:1318833, ECO:0000269|PubMed:18560155,
CC ECO:0000269|PubMed:9492318, ECO:0000269|Ref.12};
CC Note=Binds 1 hybrid [4Fe-2O-2S] cluster. {ECO:0000269|PubMed:11106482,
CC ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
CC ECO:0000269|PubMed:1318832, ECO:0000269|PubMed:1318833,
CC ECO:0000269|PubMed:18560155, ECO:0000269|PubMed:9492318};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11941509,
CC ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:1318832,
CC ECO:0000269|PubMed:18560155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069,
CC ECO:0000269|PubMed:1318832}.
CC -!- SIMILARITY: Belongs to the HCP family. {ECO:0000255|HAMAP-
CC Rule:MF_00069}.
CC -!- CAUTION: Was originally thought to contain a [6Fe-6S] cluster as
CC indicated. {ECO:0000305|PubMed:1318833}.
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DR EMBL; Z11707; CAA77767.1; -; Genomic_DNA.
DR EMBL; AE017285; AAS96488.1; -; Genomic_DNA.
DR PIR; S29861; S29861.
DR RefSeq; WP_010939296.1; NC_002937.3.
DR RefSeq; YP_011229.1; NC_002937.3.
DR PDB; 1E1D; X-ray; 1.72 A; A=1-553.
DR PDB; 1E2U; X-ray; 1.60 A; A=1-553.
DR PDB; 1E9V; X-ray; 1.72 A; A=1-553.
DR PDB; 1GNT; X-ray; 1.25 A; A=1-553.
DR PDB; 1OA1; X-ray; 1.55 A; A=1-553.
DR PDB; 1W9M; X-ray; 1.35 A; A=1-553.
DR PDBsum; 1E1D; -.
DR PDBsum; 1E2U; -.
DR PDBsum; 1E9V; -.
DR PDBsum; 1GNT; -.
DR PDBsum; 1OA1; -.
DR PDBsum; 1W9M; -.
DR AlphaFoldDB; P31101; -.
DR SMR; P31101; -.
DR STRING; 882.DVU_2013; -.
DR DrugBank; DB02761; S-Mercaptocysteine.
DR PaxDb; P31101; -.
DR PRIDE; P31101; -.
DR EnsemblBacteria; AAS96488; AAS96488; DVU_2013.
DR KEGG; dvu:DVU_2013; -.
DR PATRIC; fig|882.5.peg.1845; -.
DR eggNOG; COG1151; Bacteria.
DR HOGENOM; CLU_038344_2_0_7; -.
DR OMA; DINIYTH; -.
DR PhylomeDB; P31101; -.
DR EvolutionaryTrace; P31101; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050418; F:hydroxylamine reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01914; HCP; 1.
DR Gene3D; 1.20.1270.20; -; 2.
DR Gene3D; 3.40.50.2030; -; 2.
DR HAMAP; MF_00069; Hydroxylam_reduct; 1.
DR InterPro; IPR004137; HCP/CODH.
DR InterPro; IPR010048; Hydroxylam_reduct.
DR InterPro; IPR016099; Prismane-like_a/b-sand.
DR InterPro; IPR011254; Prismane-like_sf.
DR InterPro; IPR016100; Prismane_a-bundle.
DR PANTHER; PTHR30109; PTHR30109; 1.
DR PANTHER; PTHR30109:SF0; PTHR30109:SF0; 1.
DR Pfam; PF03063; Prismane; 1.
DR PIRSF; PIRSF000076; HCP; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR TIGRFAMs; TIGR01703; hybrid_clust; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cytoplasm; Direct protein sequencing; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..553
FT /note="Hydroxylamine reductase"
FT /id="PRO_0000151667"
FT BINDING 3
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12,
FT ECO:0000269|Ref.7"
FT BINDING 6
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12,
FT ECO:0000269|Ref.7"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12,
FT ECO:0000269|Ref.7"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12,
FT ECO:0000269|Ref.7"
FT BINDING 244
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12"
FT BINDING 268
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12"
FT BINDING 312
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12"
FT BINDING 406
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /note="via persulfide group"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12"
FT BINDING 434
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12"
FT BINDING 459
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12"
FT BINDING 494
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12"
FT BINDING 496
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11106482,
FT ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
FT ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12"
FT MOD_RES 406
FT /note="Cysteine persulfide"
FT /evidence="ECO:0000269|PubMed:11941509"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 25..50
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:1GNT"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 77..106
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 142..167
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 192..221
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:1GNT"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 385..393
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1E9V"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:1GNT"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 484..491
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 495..506
FT /evidence="ECO:0007829|PDB:1GNT"
FT STRAND 513..517
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 524..534
FT /evidence="ECO:0007829|PDB:1GNT"
FT HELIX 542..550
FT /evidence="ECO:0007829|PDB:1GNT"
SQ SEQUENCE 553 AA; 59979 MW; DC3FFC3992B51869 CRC64;
MFCFQCQETA KNTGCTVKGM CGKPEETANL QDLLIFVLRG IAIYGEKLKE LGQPDRSNDD
FVLQGLFATI TNANWDDARF EAMISEGLAR RDKLRNAFLA VYKAKNGKDF SEPLPEAATW
TGDSTAFAEK AKSVGILATE NEDVRSLREL LIIGLKGVAA YAEHAAVLGF RKTEIDEFML
EALASTTKDL SVDEMVALVM KAGGMAVTTM ALLDEANTTT YGNPEITQVN IGVGKNPGIL
ISGHDLKDMA ELLKQTEGTG VDVYTHGEML PANYYPAFKK YPHFVGNYGG SWWQQNPEFE
SFNGPILLTT NCLVPLKKEN TYLDRLYTTG VVGYEGAKHI ADRPAGGAKD FSALIAQAKK
CPPPVEIETG SIVGGFAHHQ VLALADKVVE AVKSGAIKRF VVMAGCDGRQ KSRSYYTEVA
ENLPKDTVIL TAGCAKYRYN KLNLGDIGGI PRVLDAGQCN DSYSLAVIAL KLKEVFGLDD
INDLPVSYDI AWYEQKAVAV LLALLFLGVK GIRLGPTLPA FLSPNVAKVL VENFNIKPIG
TVQDDIAAMM AGK
