ID A0A1V6PT85_9EURO Unreviewed; 1054 AA.
AC A0A1V6PT85;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=PENANT_c037G01952 {ECO:0000313|EMBL:OQD80249.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD80249.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD80249.1}.
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DR EMBL; MDYN01000037; OQD80249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PT85; -.
DR STRING; 416450.A0A1V6PT85; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000191672; 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; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
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; 2.
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:UP000191672};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 73..533
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 552..826
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 875..996
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 37..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 799
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1054 AA; 114957 MW; 94729B51DA4FBCC8 CRC64;
MAASLFALRG TRQLALRSRV RVPSIARASI SPLNLQRRGV HSSQPRGVYN STLADHGDPH
PQDIFQPLDT FPRRHIGPSP DAAGQMLAVL DPPVASLDEF VKQVLPEDIL SKKNLELSEP
HADINLYRSS VQGGLGETDM LKLLNKYREQ IDVSGKTYIG TGYYPTIVPP VIQRNVLENP
AWYTSYTPYQ PEISQGRLES LLNFQTLTAD LTGLPFANAS VLDEATAAAE AMTMSFATMP
ASKQKKADKS FVVSHLCHPQ TIAVMQSRAE GFGINLVVGD ILANDFQLVK DQKDHLIGVL
AQYPDTEGGI YDFQSLGDSI HGQGGTFSVA TDLLALTVLK APGEFGADIA FGSAQRLGVP
MGFGGPHAAF FACADKYKRK VPGRVVGVSK DRLGNRALRL ALQTREQHIR REKATSNICT
AQALLANMTA MYAIYHGPVG LKSIAERIMS MTTLLREKLV GLGYNVPLRT NGDSGVVFDT
LAVELPSAAE ADAIMAEAKA SNVFLRRLGG NKVGLSLDET VGRDEVKELL AVFAAHKSVS
PVEVDGHLGV TPIPANLERT SAYMTHPVFN THHSETEMLR YIHHLESKDL SLAHSMIPLG
SCTMKLNATS EMLPISWPEF SQIHPFMPAD KAKGYTNMID DLEQQLSDIT GMAEVTVQPN
SGAQGEFAGL RVIKKYFEGK GDAKRNLCLI PVSAHGTNPA SAAMAGMRVV TVKCDTKTGN
LDLEDLKAKC EKHKDELAAF MITYPSTFGV FEPGAKEACR LVHQHGGQVY MDGANMNAQI
GLCSPGEIGA DVCHLNLHKT FCIPHGGGGP GVGPIGVAEH LRPYLPSHPT SEYLQSKRGD
SSSPPISAAP WGSASILPIT FNYINMMGDR GLTHATKITL LNANYILSRL KPHYPILYTN
DHGRCAHEFI LDVRGFKETC GIEAIDIAKR LQDYGFHAPT MSWPVSNTLM IEPTESESKA
ELDRFCDALI SIRKEIAQVE AGEQPREGNV LKLSPHTQRD LLTTAWERPY TREKAAYPVP
YLLEKKFWPT VTRVDDAFGD QNLFCTCGPV EDSE
//
