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Database: UniProt
Entry: A0A372RN38_9GLOM
LinkDB: A0A372RN38_9GLOM
Original site: A0A372RN38_9GLOM 
ID   A0A372RN38_9GLOM        Unreviewed;      1018 AA.
AC   A0A372RN38;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE            EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN   ORFNames=C1646_636044 {ECO:0000313|EMBL:RGB42303.1};
OS   Rhizophagus sp. MUCL 43196.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB42303.1, ECO:0000313|Proteomes:UP000263633};
RN   [1] {ECO:0000313|EMBL:RGB42303.1, ECO:0000313|Proteomes:UP000263633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB42303.1,
RC   ECO:0000313|Proteomes:UP000263633};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) 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:ARBA00033655,
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:RGB42303.1}.
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DR   EMBL; QKKE01000025; RGB42303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372RN38; -.
DR   STRING; 1803374.A0A372RN38; -.
DR   InParanoid; A0A372RN38; -.
DR   Proteomes; UP000263633; 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:UP000263633};
KW   Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT   DOMAIN          75..503
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          838..959
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         766
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   1018 AA;  112817 MW;  795F9B1CBBB8C98D CRC64;
     MFFRTVHRGT KPPFVLSRRI RTITTRFNNI SVQQLDLNQI KSNQSHVSNF PKSFRKFSST
     PLKYDAFSPL DTFPRRHIGP SDAEIKAMLE TIDVKDMEEL VLKTVPANIR SKDALALEEG
     LTESELMERL KRIASKNKVY KSYIGMGYAN TIVPSVILRN VLESPGWYTQ YTPYQPEISQ
     GRLESLLNFQ TMVTDLTGMD LANASLLDEG TAAAEAMLIS FSARKQKCKT FFVDKRCHPQ
     TIACLQTRSE GFGINVIVGD ALKYDFENKH KNDLAGVLVQ YPATDGNIND YSDFSARIHS
     LGGQVVCATD LLALTLLIPP GEWGADIAVG NSQRFGVPLG YGGPHAAFFA CKDQLKRRMP
     GRLVGVSRDA SGNKAYRLSL QTREQHIRRE KATSNICTAQ ALLANMAAMY AIYHGPEGIT
     AIAKRIHNLT TALVEEIKQM GYFIKNEAFF DTLNVHIEGG ADDIIQKALN SNINFRRVDN
     NTVGITLDET VLKEDVLDII QIFSKDSNKK SNLGVPDKPN IPQKFIRTSQ FMQHQVFNSY
     HSETEMLRYI YHLQSKDLSL AHSMIPLGSC TMKLNATTEM IPITWPEFAN IHPFVPAYQA
     EGYKILIKEL EHDLAVITGF DGISLQPNSG AQGEYTGLRI IGAYHKSKGD DKRNVCLIPV
     SAHGTNPASA AMAGMEVVPV KCENNGDLDM KDLEEKATKF KDRLAAFMVT YPSTFGVFES
     GVVKACEIIH QNGGQVYMDG ANLNAQIGLC TPAGIGADVC HLNLHKTFCI PHGGGGPGVG
     PVGVKSHLMP FLPGHPVVKT GGDKCIGPVS AAPFGSPNIL PISWAYIKMM GSKGLTSATH
     IALLNANYMA VRLSNHYKIL YTNQQRMCAH EFIIDIRPFQ KTAEIEAIDI AKRLQDYGFH
     SPTMSWPVAN TLMVEPTESE SKAELDRFCD AMISIREEIK SIENGQQPKG NNILTNSPHA
     IETLIKTTWD KAYSREQAAF PLNYLKTHKF WPSVGRLDDA FGDRNLICSC PPVEDYLE
//
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