ID A0A0N8KD28_9RHOB Unreviewed; 436 AA.
AC A0A0N8KD28;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Sulfopropanediol 3-dehydrogenase HpsN {ECO:0000313|EMBL:KPQ07378.1};
GN Name=hpsN {ECO:0000313|EMBL:KPQ07378.1};
GN ORFNames=HLUCCA12_06070 {ECO:0000313|EMBL:KPQ07378.1};
OS Rhodobacteraceae bacterium HLUCCA12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ07378.1, ECO:0000313|Proteomes:UP000050476};
RN [1] {ECO:0000313|EMBL:KPQ07378.1, ECO:0000313|Proteomes:UP000050476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ07378.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPQ07378.1}.
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DR EMBL; LJSV01000004; KPQ07378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8KD28; -.
DR STRING; 1666916.HLUCCA12_06070; -.
DR PATRIC; fig|1666916.3.peg.1381; -.
DR Proteomes; UP000050476; Unassembled WGS sequence.
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: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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000099-4}.
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
SQ SEQUENCE 436 AA; 47045 MW; 48627E119365D388 CRC64;
MTVTYLKSAK PDAERAEDDA RVRATVEATL ADIESRGDAA VRELSEKFDG FSRPSFRLTD
SEIEAAMQKV STRDMADIRF AQTQIRRFAE AQRATMTDLE VETLPGIVLG HRNIPVQSVG
CYVPGGKFPM VASAHMSVLT ASVAGVPRIV ASAPPVKGEP HPAIVAAMKE GGAHEIYVLG
GIQAVGAMAL GTETIEPVHM LVGPGNAFVA EAKRQLYGRV GIDLFAGPTE TMVIADETVD
AELCATDLLG QAEHGYNSPA CMITNSRPLA EATLAEIDRL LAILPTAETA AASWRDYGEM
ILCDDHDAML RVANEKAYEH VQVMTDRDDW YLENMHSYGA LFLGPRTNVA NGDKVIGTNH
TLPTKKAGRY TGGLWVGKFL KTHSYQRITS DAAAADMAAY GSRLCMLEGF VGHAEQCNIR
LRRYGGRNVP FGTAAD
//
