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Entry: D3SB04_THISK
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ID   D3SB04_THISK            Unreviewed;       452 AA.
AC   D3SB04;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE            EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
GN   Name=gcvPA {ECO:0000256|HAMAP-Rule:MF_00712};
GN   OrderedLocusNames=TK90_1718 {ECO:0000313|EMBL:ADC72209.1};
OS   Thioalkalivibrio sp. (strain K90mix).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC72209.1, ECO:0000313|Proteomes:UP000009099};
RN   [1] {ECO:0000313|Proteomes:UP000009099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT   "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADC72209.1, ECO:0000313|Proteomes:UP000009099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K90mix {ECO:0000313|EMBL:ADC72209.1,
RC   ECO:0000313|Proteomes:UP000009099};
RX   PubMed=22675584; DOI=10.4056/sigs.2315092;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Foster B., Sun H.,
RA   Ivanova N., Pati A., D'haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of Thioalkalivibrio sp. K90mix.";
RL   Stand. Genomic Sci. 5:341-355(2011).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein binds the alpha-amino group of glycine through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       H protein. {ECO:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC       Rule:MF_00712}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00712};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_00712}.
CC   -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00712}.
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DR   EMBL; CP001905; ADC72209.1; -; Genomic_DNA.
DR   RefSeq; WP_012983085.1; NC_013889.1.
DR   AlphaFoldDB; D3SB04; -.
DR   STRING; 396595.TK90_1718; -.
DR   KEGG; tkm:TK90_1718; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000009099; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 1.
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); 1.
DR   HAMAP; MF_00712; GcvPA; 1.
DR   InterPro; IPR023010; GcvPA.
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   PANTHER; PTHR42806; GLYCINE CLEAVAGE SYSTEM P-PROTEIN; 1.
DR   PANTHER; PTHR42806:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   PIRSF; PIRSF006815; GcvPA; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00712}.
FT   DOMAIN          3..442
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
SQ   SEQUENCE   452 AA;  48913 MW;  E97148E8376ADBE9 CRC64;
     MPFIPHTEED IRSMLDRIGA DSIEDLFDEI PKELRAPALE KVPEGLNEMA ISRLMQERAA
     RDGMASNFIG AGAYEHHIPA AVWQIATRGE FYSAYTPYQA EASQGTLQLI YEYQTMISRL
     TGMEASNASL YDGASALAEA VLMAVRVNRR SKSKKILVPG ALHPDYRRVI HTLIGNQGIE
     LVEIPFDETS GQTPVDALAP FADDDVTAMI ISQPNFFGIL EDVDALTGWA EQREVPVIAV
     VNPVSLALLK PPGEWGENGV DIVVGEGQPL GAPLSSGGPY FGFMTTRKKH IRQMPGRIVG
     RAEDADGKPG YVLTLQAREQ HIRRSKATSN ICTNQGLVVT AATIHMSMLG DEGLTRVAEA
     CYANTHALVE KLAAKGIKPR FTGEYFHEVA LDFGGDAAGR VQAMADAGVL AGYQLGRDYA
     QLDGCVLACA TETKTDADLE QYVTTCEQAK AA
//
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