ID   GCSP_TROWT              Reviewed;         968 AA.
AC   Q83GV1;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
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}; Synonyms=gcvB;
GN   OrderedLocusNames=TWT_135;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Tropherymataceae;
OC   Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
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; AE014184; AAO44232.1; -; Genomic_DNA.
DR   RefSeq; WP_011102376.1; NC_004572.3.
DR   AlphaFoldDB; Q83GV1; -.
DR   SMR; Q83GV1; -.
DR   STRING; 203267.TWT_135; -.
DR   KEGG; twh:TWT_135; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_11; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000002200; 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   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; IPR000192; Aminotrans_V_dom.
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:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..968
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166944"
FT   MOD_RES         717
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   968 AA;  106422 MW;  822D3C136DDC71B5 CRC64;
     MHERHIGPSQ EEIDHMLGFL GYKSLDDLMN AALPNGVQSP PDIKIPSHDE LTCLTQLAAY
     AKMNRIKTSM LGQGFYNCIT PAVIRRNILE NPSWYTSYTP YQPEISQGRL EMLINFQTMI
     CDLTGLEIAN ASMLDEASCA AEAMLLAKRV SRSSSNKYLV HNGVFPHIRR VLETRADAVG
     VEIVDLPEGQ SIDFDHFGVY AQYQSASGKL LDLRHLFSRS KRAGAICVIG CDLLMLTLFT
     SPGELGADIA FGSAQRFGIP MNFGGPLASF LAARKAMERS LPGRLVGVSV DADSNHAYRL
     TLQTREQHIR REKATSNICT ATVLMAIAAV AFAQHHGPKG LRAIAHRINT VAVGFARLLK
     QTAFRVSSLD IFDTIEINNP TQLCVEAESK HDLLFWKVDD NKLRITFDEV TARLDGDLPE
     RLSKVFGISP DKIRDLGCNY DSCDCSFYSD SQQAREGLSS VASRNISVHS DLARHPLRRF
     SGYLKHPVFN NYTGEVALMR YLKALSDKDF ALDRGMIPLG SCTMKLNAAF QLEPVLWPEF
     ANLHPFAPRG DADGTLQIID QIETWLANLS GYDAVSLQPT AGSQGELAGL LAIRGYYKSL
     NLDRDVCLIP ASAHGTNAAS AVLAGMRVVV VACDQQGNID LDDLRLKASK NAHALAALMV
     TYPSTHGVYE DNISEVCSVV HKYGGQVYVD GANSNALIGY LRTGDFGGDV SHLNLHKTFG
     IPHGGGGPGI GPVVAKAHLA PFLPFRNRVH KPSTDLPAVK HMGGPIASSD YGFAGALYIS
     WAYIFCLGSQ GMKRCTAVAV LVANYIAKQL SDTFPVLYTG KNNLVAHEFI MDFREVTRVS
     GITVDDVCKR LIDYGFHAPT MSFPVPGTLM VEPTESEPFS EIQRFIKTIR SIRAEIDRVI
     DKTYDPDNNP LKRAPHTLEQ IASDKWDRPY SRRTGIVYTS GKYWPASARI DNAYGDRNIF
     CTCPDLPD
//