ID A0A090BVZ2_9GAMM Unreviewed; 435 AA.
AC A0A090BVZ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Histidinol dehydrogenase {ECO:0000313|EMBL:BAP57701.1};
GN ORFNames=THII_3404 {ECO:0000313|EMBL:BAP57701.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP57701.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP57701.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|PIRNR:PIRNR000099,
CC ECO:0000256|RuleBase:RU004175}.
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DR EMBL; AP014633; BAP57701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090BVZ2; -.
DR STRING; 40754.THII_3404; -.
DR KEGG; tig:THII_3404; -.
DR HOGENOM; CLU_006732_3_0_6; -.
DR Proteomes; UP000031623; Chromosome.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|PIRSR:PIRSR000099-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000099};
KW Reference proteome {ECO:0000313|Proteomes:UP000031623};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
SQ SEQUENCE 435 AA; 47377 MW; AA757DA4376BD1EC CRC64;
MMKINFYELE QLSPTETAKL FKRSELDIAA LQPTVQPIIQ AVRDQGDVAL IEYNEKFDKA
KMTVTQLKVT EAEFEQARQN LDPKIKEVIQ ISAANIKKFH QAQMPEDLWF TQIDEGIMAG
EKITPIASVG IYVPRGKGSF PSVMLMLCIP AVIAQVPKII VCTPPTAEGK VDDASLFTAE
ICGVKEVYKV GGAQAIAAMA LGTETIPKMH KVLGPGNSYV SAAKRMLYGT IDVGTPAGPS
ESIILCDEAV DPRIAALDLL IEAEHGPDST ALLVTHSREI AHQVKEHLPS LIDDLPEERQ
RFCQTVLANY GGIVLTSSLA ASLQFVNDFA PEHLEVLVKE PFAVLSKIVN AGEILLGPHT
PITLGNFSLG VNAILPTGGF AKTFSCVTVY DFLKRSSIGY VTQTGYDKLK EVARQFAEYE
GFPSHANAIS KRYSN
//
