ID A0A0Q5ZGD7_9BURK Unreviewed; 440 AA.
AC A0A0Q5ZGD7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Histidinol dehydrogenase {ECO:0000313|EMBL:KQT13163.1};
DE EC=1.1.1.23 {ECO:0000313|EMBL:KQT13163.1};
GN ORFNames=ASG30_21060 {ECO:0000313|EMBL:KQT13163.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT13163.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT13163.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13163.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT13163.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13163.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000099-4};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000099-4};
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
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:KQT13163.1}.
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DR EMBL; LMQL01000005; KQT13163.1; -; Genomic_DNA.
DR RefSeq; WP_055893652.1; NZ_LMQL01000005.1.
DR AlphaFoldDB; A0A0Q5ZGD7; -.
DR STRING; 1736365.ASG30_21060; -.
DR OrthoDB; 9805269at2; -.
DR Proteomes; UP000051173; Unassembled WGS sequence.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-EC.
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:SF14; HISTIDINOL DEHYDROGENASE; 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 ECO:0000256|PIRSR:PIRSR000099-4}; NAD {ECO:0000256|PIRSR:PIRSR000099-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000099};
KW Reference proteome {ECO:0000313|Proteomes:UP000051173};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000099-4}.
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
SQ SEQUENCE 440 AA; 48188 MW; 3B65BE16D543648A CRC64;
MIRYLKRGRD VQARTADDTK VRATVEGIIR DIEQRGDEAV REYSRKFDNW DPQDFRLSQS
QIEASIKSLS ARELEDIRFA QAQIRNFAQI QRDSMRDVEV ETRPGVFLGH RHIPVNAVGC
YVPGGKYPMI ASAHMSALTA KVAGVKRIVS TAPPFQGAPH PAIVAAMHLA GADEILVLGG
VQAVVAMAVG TPSLKPVDML VGPGNMFVAE AKRQLFGRVG IDLFAGPTET LVIADDSVDG
ELVAVDLLGQ AEHGATSPSV LLTDSEALAR DTMAEIERQL KVLPTAAIAA QSWAEFGEVI
VCDTREEMLH KADELASEHV QVMTREPDYF LDNMTNYGAL FIGPRTNVAY GDKVIGTNHT
LPTNKAARYT GGLWVGKFLK TCTFQKVVTD QASAEIGEYC SRLCHMENFA GHGEQANIRV
RRYGTRPEVP WYEPVPALDA
//
