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Database: UniProt
Entry: A0A2I0NP93_9EURY
LinkDB: A0A2I0NP93_9EURY
Original site: A0A2I0NP93_9EURY 
ID   A0A2I0NP93_9EURY        Unreviewed;       341 AA.
AC   A0A2I0NP93;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   08-MAY-2019, entry version 11.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
DE            Short=GAPDH {ECO:0000256|HAMAP-Rule:MF_00559};
DE            EC=1.2.1.59 {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
DE   AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559};
GN   Name=gap {ECO:0000256|HAMAP-Rule:MF_00559};
GN   ORFNames=CVV35_08070 {ECO:0000313|EMBL:PKL55804.1};
OS   Methanomicrobiales archaeon HGW-Methanomicrobiales-6.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales.
OX   NCBI_TaxID=2013822 {ECO:0000313|EMBL:PKL55804.1, ECO:0000313|Proteomes:UP000233331};
RN   [1] {ECO:0000313|EMBL:PKL55804.1, ECO:0000313|Proteomes:UP000233331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGW-Methanomicrobiales-6 {ECO:0000313|EMBL:PKL55804.1};
RX   PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA   Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y.,
RA   Anantharaman K., Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT   "Potential for microbial H2 and metal transformations associated with
RT   novel bacteria and archaea in deep terrestrial subsurface sediments.";
RL   ISME J. 11:1915-1929(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = 3-
CC         phospho-D-glyceroyl phosphate + H(+) + NADH;
CC         Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:59776; EC=1.2.1.59; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
CC         ECO:0000256|SAAS:SAAS01127777};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = 3-
CC         phospho-D-glyceroyl phosphate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:10296, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:59776; EC=1.2.1.59; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00559, ECO:0000256|SAAS:SAAS01127759};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
CC       ECO:0000256|SAAS:SAAS01167718}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00559,
CC       ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176914}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559,
CC       ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176915}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_00559,
CC       ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176910}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PKL55804.1}.
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DR   EMBL; PGYH01000072; PKL55804.1; -; Genomic_DNA.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000233331; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   HAMAP; MF_00559; G3P_dehdrog_arch; 1.
DR   InterPro; IPR000846; DapB_N.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01113; DapB_N; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01546; GAPDH-II_archae; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000233331};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176917};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01167717};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
KW   ECO:0000256|SAAS:SAAS01176916};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
KW   ECO:0000256|SAAS:SAAS01167721};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176912}.
FT   DOMAIN        2    140       Gp_dh_N. {ECO:0000259|SMART:SM00846}.
FT   NP_BIND      11     12       NAD. {ECO:0000256|HAMAP-Rule:MF_00559,
FT                                ECO:0000256|PIRSR:PIRSR000149-3}.
FT   REGION      139    141       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   REGION      194    195       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   ACT_SITE    140    140       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00559, ECO:0000256|PIRSR:PIRSR000149-
FT                                1}.
FT   BINDING     110    110       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   BINDING     168    168       NAD. {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   BINDING     302    302       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
SQ   SEQUENCE   341 AA;  37274 MW;  B024BBFDD8773197 CRC64;
     MIKVAINGYG TIGKRVADAV VAQPDMEVIG VSKTSVSAEA YIAKERGFPL YIADLSKREA
     FEKAGIEVAG DVDAMLKAAD VIVDATPGGV GEKNRPIYEK LGKKAIFQGG EDHEVAGFSF
     NAHANYNEAE GHQFARVVSC NTTGLVRVIH AMDQAFGVER VRAVMVRRGA DPDDVKKGPI
     DAIVLNPASI PSHHGPDLQT VLPHINIVTL AMIVPTTFMH MHSIQMDLKK ETTRDEVLKV
     FENHSRIGLV RKTMGIKSNA QLREYTQDLG RPRTDLWENG VFEESVSILD GKEFYCFQAI
     HQEADVVPEN IDCIRALVGT VKDPEESIRM TNEALGLVAI G
//
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