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Database: UniProt
Entry: A3CVY1_METMJ
LinkDB: A3CVY1_METMJ
Original site: A3CVY1_METMJ 
ID   A3CVY1_METMJ            Unreviewed;       325 AA.
AC   A3CVY1;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=NAD-dependent glycerol-3-phosphate dehydrogenase domain protein {ECO:0000313|EMBL:ABN57531.1};
GN   OrderedLocusNames=Memar_1602 {ECO:0000313|EMBL:ABN57531.1};
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407 {ECO:0000313|EMBL:ABN57531.1, ECO:0000313|Proteomes:UP000002146};
RN   [1] {ECO:0000313|EMBL:ABN57531.1, ECO:0000313|Proteomes:UP000002146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1
RC   {ECO:0000313|Proteomes:UP000002146};
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC       ECO:0000256|RuleBase:RU000437}.
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DR   EMBL; CP000562; ABN57531.1; -; Genomic_DNA.
DR   RefSeq; WP_011844442.1; NC_009051.1.
DR   AlphaFoldDB; A3CVY1; -.
DR   STRING; 368407.Memar_1602; -.
DR   GeneID; 76729670; -.
DR   KEGG; mem:Memar_1602; -.
DR   eggNOG; arCOG00456; Archaea.
DR   HOGENOM; CLU_033449_0_0_2; -.
DR   OrthoDB; 107040at2157; -.
DR   Proteomes; UP000002146; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006168; G3P_DH_NAD-dep.
DR   InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11728:SF33; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 3, CYTOSOLIC-RELATED; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000437}.
FT   DOMAIN          4..154
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          178..317
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT   BINDING         9..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         253..254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         253
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ   SEQUENCE   325 AA;  35500 MW;  60740F55194967A6 CRC64;
     MISKVGVIGA GSMGTAVAQS ISRRVGEVIV FGRRQEIVDS INTDNCNKRY FPGLRLNPNI
     HARLMGDRQG LADCEAVIIA VPSSEVRFIV NATHDELTGK FLVTVAKGLE YPSLKTMSEI
     IRDETGNPDI ACFSGPTFAD EVAYGHIAGA TIGAGGDPSL RATISNLFGE FILDFSDDIR
     AVELCGVLKN VYAIGTGMWD SVYGNHNEHY TFLNMCYKEM CIFLRAISRD KGIFTKFCCF
     GDFNLTANVD KSRNRTLGLM VGKKIVKTPY LESGVTFEGS RSVKGIIELA ENHSIDMPIA
     RFVYDVLSGN NNVRESVDGV IRKAP
//
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