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Database: UniProt
Entry: A0A2I0P482_9EURY
LinkDB: A0A2I0P482_9EURY
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ID   A0A2I0P482_9EURY        Unreviewed;       341 AA.
AC   A0A2I0P482;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   08-MAY-2019, entry version 10.
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=CVV31_13410 {ECO:0000313|EMBL:PKL61059.1};
OS   Methanomicrobiales archaeon HGW-Methanomicrobiales-2.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales.
OX   NCBI_TaxID=2013818 {ECO:0000313|EMBL:PKL61059.1, ECO:0000313|Proteomes:UP000233573};
RN   [1] {ECO:0000313|EMBL:PKL61059.1, ECO:0000313|Proteomes:UP000233573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGW-Methanomicrobiales-2 {ECO:0000313|EMBL:PKL61059.1};
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:PKL61059.1}.
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DR   EMBL; PGYL01000051; PKL61059.1; -; Genomic_DNA.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000233573; 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:UP000233573};
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;  37030 MW;  3D28C947AD1AA37C CRC64;
     MIKVAINGYG TIGKRVADAV AAQPDMEVIG VSKTSVSAEA FIAKERGYPL YIADLAKKPA
     FEKAGIEVAG DVAAMLKAAD IVVDATPGGV GEKNKPIYER LGKKAIWQGG EAHEVAGFSF
     NAHANYKEAA GKQFARVVSC NTTGLVRIIN AMDQAFGVER VRAVMVRRGA DPSDVKRGPI
     DAIVLNPATI PSHHGPDVQT VLPHINIVTL AMIVPTTFMH MHSIQMDLKK ETTRDEVLKV
     FEDHSRIGLV RKATGIKSNA ELREYTQDLG RPRTDLWENG VFEESVSVLN GKEFYCFQAI
     HQEADVIPEN IDCIRALMGT VKDPQESIRM TNKALGLVAI G
//
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