HCP_DESDA
ID HCP_DESDA Reviewed; 545 AA.
AC Q01770; B8J267;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
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=Ddes_1829;
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1511014; DOI=10.1016/0167-4781(92)90057-7;
RA Stokkermans J.P.W.G., van den Berg W.A.M., 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 desulfuricans (ATCC 27774).";
RL Biochim. Biophys. Acta 1132:83-87(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-37, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RX PubMed=1311311; DOI=10.1016/s0021-9258(18)42859-1;
RA Moura I., Tavares P., Moura J.J.G., Ravi N., Huynh B.H., Liu M.Y.,
RA le Gall J.;
RT "Direct spectroscopic evidence for the presence of a 6Fe cluster in an
RT iron-sulfur protein isolated from Desulfovibrio desulfuricans (ATCC
RT 27774).";
RL J. Biol. Chem. 267:4489-4496(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR
RP CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SULFHYDRATION AT CYS-400,
RP AND SUBUNIT.
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR
RP CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, AND COFACTOR.
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RX PubMed=14646063; DOI=10.1107/s0907444903025861;
RA Macedo S., Aragao D., Mitchell E.P., Lindley P.;
RT "Structure of the hybrid cluster protein (HCP) from Desulfovibrio
RT desulfuricans ATCC 27774 containing molecules in the oxidized and reduced
RT states.";
RL Acta Crystallogr. D 59:2065-2071(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR
RP CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
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).
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:11941509, ECO:0000269|PubMed:12764602,
CC ECO:0000269|PubMed:1311311, ECO:0000269|PubMed:14646063};
CC Note=Binds 1 spin-admixed [4Fe-4S] cluster.
CC {ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
CC ECO:0000269|PubMed:1311311, ECO:0000269|PubMed:14646063};
CC -!- COFACTOR:
CC Name=hybrid [4Fe-2O-2S] cluster; Xref=ChEBI:CHEBI:60519;
CC Evidence={ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602,
CC ECO:0000269|PubMed:14646063};
CC Note=Binds 1 hybrid [4Fe-2O-2S] cluster. {ECO:0000269|PubMed:11941509,
CC ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11941509,
CC ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:1311311}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069}.
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:1311311}.
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DR EMBL; Z11975; CAA78029.1; -; Genomic_DNA.
DR EMBL; CP001358; ACL49726.1; -; Genomic_DNA.
DR PIR; S24389; S24389.
DR RefSeq; WP_012625450.1; NC_011883.1.
DR PDB; 1GN9; X-ray; 2.60 A; A/B=2-545.
DR PDB; 1GNL; X-ray; 1.25 A; A/B=2-545.
DR PDB; 1OA0; X-ray; 1.25 A; A/B=2-545.
DR PDB; 1UPX; X-ray; 1.25 A; A/B=2-545.
DR PDBsum; 1GN9; -.
DR PDBsum; 1GNL; -.
DR PDBsum; 1OA0; -.
DR PDBsum; 1UPX; -.
DR AlphaFoldDB; Q01770; -.
DR SMR; Q01770; -.
DR STRING; 525146.Ddes_1829; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB02761; S-Mercaptocysteine.
DR PRIDE; Q01770; -.
DR EnsemblBacteria; ACL49726; ACL49726; Ddes_1829.
DR KEGG; dds:Ddes_1829; -.
DR eggNOG; COG1151; Bacteria.
DR HOGENOM; CLU_038344_2_0_7; -.
DR OMA; DINIYTH; -.
DR OrthoDB; 337713at2; -.
DR EvolutionaryTrace; Q01770; -.
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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1311311"
FT CHAIN 2..545
FT /note="Hydroxylamine reductase"
FT /id="PRO_0000151666"
FT BINDING 7
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063"
FT BINDING 10
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063"
FT BINDING 241
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063"
FT BINDING 265
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063"
FT BINDING 309
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063"
FT BINDING 400
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /note="via persulfide group"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602"
FT BINDING 428
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063"
FT BINDING 453
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063"
FT BINDING 488
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:14646063"
FT BINDING 490
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000269|PubMed:11941509,
FT ECO:0000269|PubMed:14646063"
FT MOD_RES 400
FT /note="Cysteine persulfide; in oxidized form"
FT /evidence="ECO:0000269|PubMed:11941509"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1OA0"
FT HELIX 29..54
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:1GNL"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 82..101
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:1GNL"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 138..163
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 189..218
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:1GNL"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 372..377
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 379..387
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 408..416
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:1GNL"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 456..469
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 478..485
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 489..500
FT /evidence="ECO:0007829|PDB:1GNL"
FT STRAND 507..511
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 518..528
FT /evidence="ECO:0007829|PDB:1GNL"
FT HELIX 536..542
FT /evidence="ECO:0007829|PDB:1GNL"
SQ SEQUENCE 545 AA; 58659 MW; FEFF010FF9FBE4AC CRC64;
MSNAMFCYQC QETVGNKGCT QVGVCGKKPE TAALQDALIY VTKGLGQIAT RLRAEGKAVD
HRIDRLVTGN LFATITNANF DDDILAERVR MTCAAKKELA ASLTDKSGLS DAALWEASEK
SAMLAKAGTV GVMATTDDDV RSLRWLITFG LKGMAAYAKH ADVLGKHENS LDAFMQEALA
KTLDDSLSVA DLVALTLETG KFGVSAMALL DAANTGTYGH PEITKVNIGV GSNPGILISG
HDLRDLEMLL KQTEGTGVDV YTHSEMLPAH YYPAFKKYAH FKGNYGNAWW KQKEEFESFN
GPVLLTTNCL VPPKDSYKDR VYTTGIVGFT GCKHIPGEIG EHKDFSAIIA HAKTCPAPTE
IESGEIIGGF AHNQVLALAD KVIDAVKSGA IKKFVVMAGC DGRAKSRSYY TDFAEGLPKD
TVILTAGCAK YRYNKLNLGD IGGIPRVLDA GQCNDSYSLA VIALKLKEVF GLEDVNDLPI
VYNIAWYEQK AVIVLLALLS LGVKNIHLGP TLPAFLSPNV AKVLVEQFNI GGITSPQDDL
KAFFG
