ID A0A139D805_9FIRM Unreviewed; 433 AA.
AC A0A139D805;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ORFNames=AWL62_1049 {ECO:0000313|EMBL:KXS49450.1};
OS Halanaerobium sp. T82-1.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=1794808 {ECO:0000313|EMBL:KXS49450.1, ECO:0000313|Proteomes:UP000070487};
RN [1] {ECO:0000313|EMBL:KXS49450.1, ECO:0000313|Proteomes:UP000070487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T82-1 {ECO:0000313|EMBL:KXS49450.1};
RA Wolfe R., Daly R., Wrighton K.;
RT "Halanaerobium-1 T82 Annotated.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXS49450.1}.
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DR EMBL; LSBN01000035; KXS49450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139D805; -.
DR PATRIC; fig|1794808.3.peg.872; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000070487; Unassembled WGS sequence.
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 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 ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 132
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 194
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 217
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 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 262
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 262
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 265
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 265
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 364
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 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 423
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 423
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
SQ SEQUENCE 433 AA; 47169 MW; 343FFBF1D01E9366 CRC64;
MLKIKRIKDG RKNVEQVKEL LDSRSGDNLA KYRDVAADIL KRVRESGDQA VLDYTARFDG
IEFEASELEV TEIEIRAALK EVDADFIEAL KNAAANIEEF HAEQKDKSWQ KQKKPGIITG
QVCRPLKKAG VYVPGGRAAY PSSVLMTVIP AKVAGVEEII MFTPPDKEGK VSPVILAAAE
IAGADRIFKV GGAQAVAAAA YGTETIPGVD IIVGPGNIYV SMAKELVFGQ VKIDMIAGPS
EIMIMAEKES NPAYIAADLM SQAEHDPLAS SILVTDAPEL IEKVEAELEK QIEKMSNKEI
IKESLENFGL MIEVKNPEAA MEMINLVAPE HLELAVKNPF ELLPAVENAG SIFLGEYTPE
PIGDYYAGPN HVLPTNSTAR FFSPLSVRDF VKYSGFIHYS KAALKEASND VICLAEGEGL
DAHANSVRIR KQK
//
