ID A0A0N8K600_9RHOB Unreviewed; 428 AA.
AC A0A0N8K600;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Sulfopropanediol 3-dehydrogenase HpsN {ECO:0000313|EMBL:KPP87553.1};
GN Name=hpsN {ECO:0000313|EMBL:KPP87553.1};
GN ORFNames=HLUCCA08_17270 {ECO:0000313|EMBL:KPP87553.1};
OS Rhodobacteraceae bacterium HLUCCA08.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666913 {ECO:0000313|EMBL:KPP87553.1, ECO:0000313|Proteomes:UP000050293};
RN [1] {ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
RN [2] {ECO:0000313|EMBL:KPP87553.1, ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA08 {ECO:0000313|EMBL:KPP87553.1};
RX PubMed=26497460; DOI=10.1128/AEM.02274-15;
RA Nelson W.C., Maezato Y., Wu Y.W., Romine M.F., Lindemann S.R.;
RT "Identification and Resolution of Microdiversity through Metagenomic
RT Sequencing of Parallel Consortia.";
RL Appl. Environ. Microbiol. 82:255-267(2016).
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:KPP87553.1}.
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DR EMBL; LJSF01000027; KPP87553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8K600; -.
DR STRING; 1666913.HLUCCA08_17270; -.
DR PATRIC; fig|1666913.4.peg.1468; -.
DR Proteomes; UP000050293; 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 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 252
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 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 428 AA; 45531 MW; 5E7C18EC4842A78C CRC64;
MTLRPLKTAA PRPITESADL RDTVAIMLAD IARDGEARVR RYAETLDRWT GPIVLPDDAR
RAAIERVPQA LRDRIAFAHD NIRRFAEAQR ATLTDMEVEL SPGHVAGQKS IPVDSAGCYV
PGGRYAHIAS ALMSVTTARA AGVPHVTAAT PPRGGQGIPD AIIYAMDLAG ADSILTLGGV
QGIAAMAEGL FGLPPADILV GPGNAYVAEA KRQLFGRVGI DMVAGPTDSL VIADSSADAE
TVAWDLIGQA EHGPDSPVWL VTDHEPLARQ VMALAPRLAE TLAEPNRSAA RIAWAERAEV
VLCDTREDMA RAADRYAPEH LHVQARDLEW WLGRLRVYGS LFLGAETTVP FGDKVAGPNH
VLPTSGAARY TGGLSVHKFL KTVTWQRCDT AAGARLAEAA TLICTEEGME GHARSAALRL
ARPIPAGA
//
