ID   GCSP_AROAE              Reviewed;         972 AA.
AC   Q5NZ93;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
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}; OrderedLocusNames=AZOSEA34960;
GN   ORFNames=ebA6124;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(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=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC         glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC         [glycine-cleavage complex H protein] + CO2; 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; CR555306; CAI09621.1; -; Genomic_DNA.
DR   RefSeq; WP_011239280.1; NC_006513.1.
DR   AlphaFoldDB; Q5NZ93; -.
DR   SMR; Q5NZ93; -.
DR   STRING; 76114.ebA6124; -.
DR   EnsemblBacteria; CAI09621; CAI09621; ebA6124.
DR   KEGG; eba:ebA6124; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_4; -.
DR   OMA; DEHCHPQ; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000006552; 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; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
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   PANTHER; PTHR11773; PTHR11773; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..972
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227090"
FT   MOD_RES         713
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   972 AA;  103927 MW;  8B37141C4012F18B CRC64;
     MPNASPASPL NAPLAELEQR DAFIGRHVGP NATEIATMLA AVGAPDLDTL IDQTVPPAIR
     LAAPLPLEGP KPEHEALADL RAIAAKNVIR KSLIGMGYYG THTPAVILRN VMENPGWYTA
     YTPYQAEIAQ GRLEALLNYQ QMVIDLTGLE LANASLLDEA TAAAEAMTMA RRVAKSKSNV
     FYVDEACFPQ TIDVLRTRAG LFGFELKFGP AHDAANADAF GALLQYPNER GEIIDLSGTV
     AALKAKGAVV AIASDLMALV LLKSPGTMGA DIALGSAQRF GVPMGFGGPH AAFFATREAN
     VRAMPGRIIG VSKDARGKTA LRMTLQTREQ HIRREKANSN ICTSQVLLAN MSGFYAVYHG
     PQGLRTIAAR IHRLAAILAQ GLRDAGFNVP AGAFFDTLQV DTGARTAELL AACDAAGFNL
     RPVSDTVLGL SVDETTTGDD VATLLRLFGA SGELAALDAK VGAAGGAIPA ALLRDDAILT
     HPVFNTHHTE HEMLRYLKKL QNRDLALDHS MISLGSCTMK LNATSEMIPI TWAEFANLHP
     FAPREQVRGY LEMIDGLAGY LKAVTGFAAI SMQPNSGAQG EYAGLVAIRR YHDSRGDTHR
     RVCLIPKSAH GTNPASAQMC GMDVVVVACD ERGNVDLADL EAKVAQHADR LAALMITYPS
     THGVFEESIR EICASVHRHG GQVYMDGANL NAQVGLTSPA TIGADVSHMN LHKTFCIPHG
     GGGPGMGPIG LAAHLAPFMA DHVVAATGDE TRPNKGQGAV SAAPFGSASI LPISWMYIAM
     MGDTGLKLAT EVAILNANYV ANRLAEHYPV LYTGSQGRVA HECILDIRPI KANTGISEVD
     IAKRLMDYGF HAPTMSFPVA GTIMIEPTES EDLGELDRFI AAMITIRNEI REVENGAWPT
     DDNPLKNAPH TQADFIAADG AQWSRPYSRE QAVFPLPWVA ENKFWPSVNR IDDVYGDRNL
     FCACVPIEDY AS