HISX_METCA
ID HISX_METCA Reviewed; 436 AA.
AC Q606Q2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024};
DE Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024};
DE EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024};
GN Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024}; OrderedLocusNames=MCA1963;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH;
CC Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699,
CC ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01024};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01024};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01024};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
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DR EMBL; AE017282; AAU92021.1; -; Genomic_DNA.
DR RefSeq; WP_010961209.1; NC_002977.6.
DR PDB; 4GIC; X-ray; 2.05 A; A/B=2-422.
DR PDBsum; 4GIC; -.
DR AlphaFoldDB; Q606Q2; -.
DR SMR; Q606Q2; -.
DR STRING; 243233.MCA1963; -.
DR PRIDE; Q606Q2; -.
DR EnsemblBacteria; AAU92021; AAU92021; MCA1963.
DR KEGG; mca:MCA1963; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_6; -.
DR OMA; MVTGPGN; -.
DR OrthoDB; 935289at2; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06572; Histidinol_dh; 1.
DR HAMAP; MF_01024; HisD; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR001692; Histidinol_DH_CS.
DR InterPro; IPR022695; Histidinol_DH_monofunct.
DR InterPro; IPR012131; Hstdl_DH.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PIRSF; PIRSF000099; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00069; hisD; 1.
DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Histidine biosynthesis;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..436
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135794"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 135
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 219
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 87..107
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4GIC"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:4GIC"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:4GIC"
SQ SEQUENCE 436 AA; 47045 MW; 161D3DEAAE8BDE17 CRC64;
MTEVKIKRLY TGDADFASQL DRLLAWSESE DTDIHQRVTE IIGCIRRDGD AALVELTARF
DHFVVDTAAA LELPRDVLEA AWQALPAEQA KALREAAERI RAYAERQKLD SWDYREADGT
LLGQKITPLD RVGLYVPGGK AAYPSSVLMN AVPAKVAGVP ELIMAVPAPR GELNALVLAA
AYISGVDRVF RIGGAQAVAA LAYGTETVPR VDKIVGPGNI YVATAKKLVF GQVGIDMVAG
PSEILVISDG RTDPDWIAMD LFSQAEHDED AQAILISPDA AHLEAVQASI ERLLPGMERA
EVIRTSLERR GGMILVDDLE QAAAVANRIA PEHLELSVES PEVLVESIRN AGAIFMGRYT
AEALGDYCAG PNHVLPTSGT ARFSSPLGVY DFQKRSSLIY CSPDGADQLG RTASLLAWGE
GLGAHARSAE YRIRHH
