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   16-JUN-2009, entry version 21.
DE   RecName: Full=Glycine dehydrogenase [decarboxylating] 1;
DE            EC=1.4.4.2;
DE   AltName: Full=Glycine decarboxylase 1;
DE   AltName: Full=Glycine cleavage system P-protein 1;
GN   Name=gcvP1; OrderedLocusNames=CPS_1276;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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
RT   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
CC       through its pyridoxal phosphate cofactor; CO(2) is released and
CC       the remaining methylamine moiety is then transferred to the
CC       lipoamide cofactor of the H protein (By similarity).
CC   -!- CATALYTIC ACTIVITY: Glycine + H-protein-lipoyllysine = H-protein-
CC       S-aminomethyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H (By similarity).
CC   -!- SIMILARITY: Belongs to the gcvP family.
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DR   EMBL; CP000083; AAZ27305.1; -; Genomic_DNA.
DR   RefSeq; YP_268019.1; -.
DR   GeneID; 3521561; -.
DR   GenomeReviews; CP000083_GR; CPS_1276.
DR   KEGG; cps:CPS_1276; -.
DR   NMPDR; fig|167879.3.peg.1237; -.
DR   TIGR; CPS_1276; -.
DR   HOGENOM; Q486J6; -.
DR   OMA; Q486J6; PAVNRVD.
DR   BioCyc; CPSY167879:CPS_1276-MON; -.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) act...; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavag...; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00711; -; 1.
DR   InterPro; IPR003437; GDC-P.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   PANTHER; PTHR11773; GDC-P; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN         1    965       Glycine dehydrogenase [decarboxylating]
FT                                1.
FT                                /FTId=PRO_0000227102.
FT   MOD_RES     713    713       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
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
//