ID Q2JWQ2_SYNJA Unreviewed; 437 AA.
AC Q2JWQ2;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024};
DE Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024};
DE EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024};
GN Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024,
GN ECO:0000313|EMBL:ABC98807.1};
GN OrderedLocusNames=CYA_0591 {ECO:0000313|EMBL:ABC98807.1};
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=321327 {ECO:0000313|EMBL:ABC98807.1, ECO:0000313|Proteomes:UP000008818};
RN [1] {ECO:0000313|EMBL:ABC98807.1, ECO:0000313|Proteomes:UP000008818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab {ECO:0000313|EMBL:ABC98807.1,
RC ECO:0000313|Proteomes:UP000008818};
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01024};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01024,
CC ECO:0000256|PIRSR:PIRSR000099-4};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01024,
CC ECO:0000256|PIRSR:PIRSR000099-4};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC {ECO:0000256|HAMAP-Rule:MF_01024}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|HAMAP-Rule:MF_01024,
CC ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|RuleBase:RU004175}.
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DR EMBL; CP000239; ABC98807.1; -; Genomic_DNA.
DR RefSeq; WP_011429494.1; NC_007775.1.
DR AlphaFoldDB; Q2JWQ2; -.
DR STRING; 321327.CYA_0591; -.
DR KEGG; cya:CYA_0591; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_3; -.
DR OrthoDB; 9805269at2; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000008818; 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 Gene3D; 1.20.5.1300; -; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
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 NCBIfam; TIGR00069; hisD; 1.
DR PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1.
DR PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PIRSF; PIRSF000099; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01024};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01024};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}.
FT COILED 1..28
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 219
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
SQ SEQUENCE 437 AA; 46290 MW; 39C179BDFE0A7256 CRC64;
MLRIVTQLAE AEAELRRISE RTQADQNLHR EATVREILQA VRRQGDRALL AYTAEFDQVE
LSVAELKVSG AELEAAYQAV SPQLLSALRL AKQRIEAFHR QRVPSSWVSF PGPEIVLGKQ
YRPVDRAGLY IPGGRAAYPS TVLMNAIPAK VAGVPEIVMV TPPGSDGLGG KGISPAILVA
AQEVGIHTIY RVGGAQAIGA LAYGTETIPK VDVITGPGNI YVTLAKKLVY GTVGIDSLAG
PSEVLIIADE SANPLYVAAD LLAQAEHDPL AAAILLTPDP KLAQQVQQAV TTQMEAHPNR
LLVEKAVANY GLIAVVPDLA TAVNLSNQFA PEHLELQVAD PWALLDPIRH AGAIFLGHYT
PEAVGDYLAG PNHTLPTAGA ARYASALGVE TFLKHSSLIQ YGSAALQEVA GAIQALAQAE
GLPAHGQSVQ VRLAEEH
//
