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Database: UniProt
Entry: A0A3R7MMD6_PENVA
LinkDB: A0A3R7MMD6_PENVA
Original site: A0A3R7MMD6_PENVA 
ID   A0A3R7MMD6_PENVA        Unreviewed;      1085 AA.
AC   A0A3R7MMD6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE            EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN   ORFNames=C7M84_016558 {ECO:0000313|EMBL:ROT65479.1};
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT65479.1, ECO:0000313|Proteomes:UP000283509};
RN   [1] {ECO:0000313|EMBL:ROT65479.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT65479.1};
RA   Zhang X., Yuan J., Li F., Xiang J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ROT65479.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT65479.1};
RA   Sun Y., Gao Y., Yu Y.;
RT   "The decoding of complex shrimp genome reveals the adaptation for benthos
RT   swimmer, frequently molting mechanism and breeding impact on genome.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000256|RuleBase:RU364056}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00043839,
CC         ECO:0000256|RuleBase:RU364056};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR603437-50, ECO:0000256|RuleBase:RU364056};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|RuleBase:RU364056}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU364056}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC       ECO:0000256|RuleBase:RU364056}.
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:ROT65479.1}.
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DR   EMBL; QCYY01003082; ROT65479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R7MMD6; -.
DR   STRING; 6689.A0A3R7MMD6; -.
DR   EnsemblMetazoa; XM_027372358.1; XP_027228159.1; LOC113820096.
DR   Proteomes; UP000283509; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|RuleBase:RU364056};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364056};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50,
KW   ECO:0000256|RuleBase:RU364056};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW   Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT   DOMAIN          131..553
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          900..1021
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         823
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   1085 AA;  119802 MW;  23AB48EB0B24968B CRC64;
     MPYCPEKRVS LSPSSTMYFY PVLVWRGEGE DARVKSLRVH NVAGSSRWQV AGGFAIEDTG
     SEAATDTRAA VRVARCCPVM LDHLARSQGR TVARIVARKV NRGQLGQIRS QGSAAASTTS
     LLPAADDFCV RHIGPRKDDQ KRMLESLGYE SLDALTDAAV PENIRLGRDL KVQEPIGEHA
     LLGRIREISE KNEIWRSYIG MGYHNCRVPH AILRNIFENP GWTTQYTPYQ PEVAQGRLES
     LLNYQTMVTD LTGLPVANAS LLDEGTAAAE AVGLAYRQNK RRKVYLSDKL HPQTLAVVRT
     RAIPLGLEVL IGDVFDIDFT NRDVSAVLFQ YPDTEGTVHD FTQVIENAQS NGTMVVCATD
     LLAVTVLAPP GDLGVDIAVG TSQRLGVPLG YGGPHAGFFA CKSNLVRLMP GRMIGVTRDA
     NGKDSYRLAL QTREQHIRRD KATSNICTAQ ALLANMSAMF AVYHGPKGLK DIANRIHNAT
     IILSRGLQSA GHIIENDVFF DTIRVNPTLA TSEIRMRAQQ KEINLRYFRD ETVGIALDET
     VEKQDLDDLF WVFNCKNVTA EKVASNLSGA ALPKEHISNT NFARKSDFLT HSIFNTYHSE
     AQLVRYLKTL ENKDVSLVHS MIPLGSCTMK LNSTTEMMPC SFPHFTEIHP FVPPEQALGY
     RLLFEELEHD LCEITGYDKI SFQPNSGAQG EYAGLRAIMS YLDARGEGHR NVCLIPTSAH
     GTNPASAQMA GMKVEAVNVD KEGSIDFRHL TAKIEKHRKN LACLMITYPS TNGVFEETVK
     DVCQMVHDAG GQVYLDGANM NAQVGLCRPG DIGGDVSHLN LHKTFCIPHG GGGPGMGPIG
     VKAHLVPYLP SHPIVDPMAL MKKKARSFGV VSAAPYGSAA ILPISWAYVK MMGPKGLREA
     TQVAILNANY MANRLQKYYK VLYTGNCGLV AHEFILDMRE FKKTAGIEAT DIAKRLQDYG
     FHAPTMSWPV AGSLMVEPTE SEDKAELDRF CDALILIREE IRDLEEGRSD PKCNPLNMSP
     HPLVTVTSSN WDRPYSREQA AFPAPFVRPE SKWWPTVGRI DDIYGDRNLV CTCPPMETYC
     SPFED
//
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