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
//