ID   GCSP_SHESA              Reviewed;         962 AA.
AC   A0L103;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) {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 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711};
GN   OrderedLocusNames=Shewana3_3499;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000469; ABK49722.1; -; Genomic_DNA.
DR   RefSeq; WP_011718287.1; NC_008577.1.
DR   AlphaFoldDB; A0L103; -.
DR   SMR; A0L103; -.
DR   STRING; 94122.Shewana3_3499; -.
DR   KEGG; shn:Shewana3_3499; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000002589; 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..962
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045612"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   962 AA;  104750 MW;  959747FDB5D9C343 CRC64;
     MTKQTLTQLE QHDLFLRRHI GPDSSQQQEM LNYVGAESLD DLTAQIVPES IRLSQELSIG
     DSCGEAEGIA YIRGLAKQNQ VFKSYIGMGY YGTQVPNVIL RNVFENPGWY TAYTPYQPEI
     AQGRLEAILN FQQVSMDLTG LDLASASLLD EATAAAEAMA LAKRVSKAKK ANIFFVADDV
     FPQTLDVVKT RAECFGFEVV VGPAHEAVNH ELFGALFQYS NRFGQITDFT DLFAELRAKN
     VIVTVAADIM ALVLLKSPGA MGADVVFGSA QRFGVPMGFG GPHAAFFVAR DEHKRSMPGR
     IIGVSKDTRG NRALRMAMQT REQHIRREKA NSNICTAQIL LANMASFYAV FHGPQGLKTI
     ASRINRFTDI LAAGLQAKGV SLVNNTWFDT ISIKGLDVAA VNARALAAEM NLRFDADGIV
     GVSLDETTIR TDIEALFDVI LGAGHGLDVA ALDAQIVAQG SQSIPASLVR QDAILSHPTF
     NRYQSETEMM RYIKRLESKD LALNYSMISL GSCTMKLNAA VEMIPVSWPE FANMHPFCPL
     DQAKGYTQLI EELSSWLVNV TGYDAVCIQP NSGAQGEYAG LLAIRKYHES RGEAHRNICL
     IPQSAHGTNP ASAQLAGMQV VVTACDKQGN VDLEDLKAKA AEVAENLSCI MITYPSTHGV
     YEESIREICN IVHQHGGQVY LDGANMNAQV GLTSPGFIGA DVSHLNLHKT FAIPHGGGGP
     GMGPIGVKAH LAPFVAGHVV VKPGRESDNN GAVSAAPYGS AGILPISWMY IKLLGSNGLK
     KSTQTALLNA NYVMKKLSEH YPVLFRGRND RVAHECIIDL RPIKEASGVT EMDIAKRLND
     YGFHAPTMSF PVAGTLMIEP TESESKVELD RFIDAMVSIR AEIAKVEAGE WPADNNPLHN
     APHTMADIMD PAFDSRPYSR EVAVFPSAAV RTNKFWPTVN RIDDVYGDRN LFCACVPLSD
     YE
//