ID   GCSP1_COLP3             Reviewed;         965 AA.
AC   Q486J6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) 1 {ECO:0000255|HAMAP-Rule:MF_00711};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine cleavage system P-protein 1 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase 1 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 1 {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP1 {ECO:0000255|HAMAP-Rule:MF_00711};
GN   OrderedLocusNames=CPS_1276;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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:0000255|HAMAP-Rule:MF_00711}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00711};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC       Rule:MF_00711}.
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DR   EMBL; CP000083; AAZ27305.1; -; Genomic_DNA.
DR   RefSeq; WP_011042113.1; NC_003910.7.
DR   AlphaFoldDB; Q486J6; -.
DR   SMR; Q486J6; -.
DR   STRING; 167879.CPS_1276; -.
DR   KEGG; cps:CPS_1276; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   Proteomes; UP000000547; 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   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   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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..965
FT                   /note="Glycine dehydrogenase (decarboxylating) 1"
FT                   /id="PRO_0000227102"
FT   MOD_RES         713
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   965 AA;  104676 MW;  2D76B8A433A614DB CRC64;
     MTSKTIVNSL AELEQTQDFI RRHIGPSESE TQAMLNDLGV ESVDALIDEI VPSDIRLADL
     PNVEESKTEV QALADLKAVA SLNKVNDTYI GLGYFGTLTP NVILRNVLEN PGWYTAYTPY
     QPEIAQGRLE SLLNYQQMCI DLTGLELASA SLLDEGTAAA EAMALAKRVS KNKKSNLFFI
     SDDVYPQTID VVKQRAEMFG FDIVVAPAAD AAEHDIFGAL IQYPGASGQV TDVSELIAKI
     HDNKGIVAVA ADIMSLVLLK SPGELGADAV IGSSQRFGVP MGYGGPHAAF FTTLDKYKRS
     LPGRIIGVSK DTRGKNALRM AMQTREQHIR REKANSNVCT AQVLLANMAA FYAVYHGPQG
     LKTIANRIHR LADILCLGTA TKGLTAVHAN YFDTLTFNVD NKDEIVARAL AANANFRTDV
     DGQISIALDE TTTRENVAQL FDILLGEGHG LNVSDLDDQI VASGHSSIPA SLVRESAILT
     HPVFNSYHSE TEMLRYIKRL ENKDLALNHS MISLGSCTMK LNATAQMIPV SWPEFANMHP
     FAPVNQAQGY KAMIDELAKW LVELTGYDKM SMQPNSGAQG EYAGLIAISK YHESRGDSHR
     NICLIPASAH GTNPASAMMV DMKIVIVACD KEGNVDMADL KAKAEELADN LACIMITYPS
     THGVYETTIA EICNIIHDNG GQVYLDGANM NAQVGLTSPG FIGADVSHLN LHKTFAIPHG
     GGGPGMGPIG VKSHLAPFLP DHALINVDEA TKGNGAVSSA PFGSASILPI TYLYIALLGK
     KGVTDATKYA ITNANYVSKK LSEHYPILYS GKNGRVAHEC IVDLRPLKAS SGVTEVDMAK
     RLMDYGFHSP TMSFPVAGTF MIEPTESESK VELDRFIEAM VCIRDEVRKV ESGEWASDNN
     PLHNAPHTLA DITEPWDRPY SIQEAVFPVV AVTANKFWPT VNRIDDVFGD RNLICSCPPI
     ESYID
//