ID   GCSP_SHELP              Reviewed;         962 AA.
AC   A3QHI0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 109.
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=Shew_3062;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
RG   US DOE Joint Genome Institute;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) 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; CP000606; ABO24928.1; -; Genomic_DNA.
DR   RefSeq; WP_011866858.1; NC_009092.1.
DR   AlphaFoldDB; A3QHI0; -.
DR   SMR; A3QHI0; -.
DR   STRING; 323850.Shew_3062; -.
DR   KEGG; slo:Shew_3062; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000001558; 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; 2.
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; Reference proteome.
FT   CHAIN           1..962
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045610"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   962 AA;  104745 MW;  89C34F58A2602DB0 CRC64;
     MTTETLTQLE QHELFIRRHI GPDSADQQEM LNFVGAESLE DLTQQIVPES IRLGRDLAVG
     SACGEAEGLA SIRKYADKNK VFKSYIGMGY YGTIVPSVIQ RNVFENPGWY TAYTPYQPEI
     AQGRLEAILN FQQLSMDLTG LDLASASLLD EATAAAEAMA LAKRVSKAKK ANIFFIADDV
     FPQTIDVVKT RAECFGFEIV VGPASEAVNY ELFGALFQYT NHYGQITDFT ELFAALQEKK
     AVVTVAADIM SLVSLKSPGS MGADVVFGSA QRFGVPMGFG GPHAAFFVTR DQHKRSLPGR
     IIGVSQDTRG NRALRMAMQT REQHIRREKA NSNICTAQVL LANMASFYAV FHGPQGLKII
     ADRIHRLADI FAAGLKAKGV ELVNNTWFDT VSFKVADSAA AQARAIAGEV NLRIDSDGIL
     GVAMAETTTR EDVAQLFDIV LGEGHGLDVA AIDADIIANG SNSIPAELVR QDAILEHPTF
     NRYHSETEMM RYIKRLENKD LALNHSMISL GSCTMKLNAA TEMMPVSWPE FGNMHPFCPQ
     DQAQGYAELI EELSNWLVDI TGYDAMCMQP NSGASGEYAG LLAIKKYHES RGEGHRNVCL
     IPQSAHGTNP ASAQLAGMKI VVTACDKQGN VDMEDLKAKA AEVAENLSCI MVTYPSTHGV
     YEETISEICE VIHQHGGQVY LDGANMNAQV GLTSPGSIGA DVSHLNLHKT FAIPHGGGGP
     GMGPIGVKAH LAPFVAGHAV VKHGRESDNN GAVSAAPYGS ASILPITWMY IKLLGYQGLR
     QSTQMALLNA NYVMKKLSAH YPVLYTGRND RVAHECIIDL RPLKEASGVT EMDIAKRLND
     YGFHAPTMSF PVAGTLMIEP TESESKAELD RFIEAMVAIR GEIAKVEAGE WPADNNPLHN
     APHTMADIMD SEFDSRPYSR ETAVFPTAAV KANKFWPTVN RIDDVYGDRN LMCSCAPIDD
     YK
//