ID   GCSP_AKKM8              Reviewed;         948 AA.
AC   B2UNH4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Amuc_0448;
OS   Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS   81048 / CCUG 64013 / CIP 107961 / Muc).
OC   Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=349741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC   107961 / Muc;
RX   PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA   van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA   Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT   "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT   degrader, and its use in exploring intestinal metagenomes.";
RL   PLoS ONE 6:E16876-E16876(2011).
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; CP001071; ACD04286.1; -; Genomic_DNA.
DR   RefSeq; WP_012419501.1; NC_010655.1.
DR   AlphaFoldDB; B2UNH4; -.
DR   SMR; B2UNH4; -.
DR   STRING; 349741.Amuc_0448; -.
DR   EnsemblBacteria; ACD04286; ACD04286; Amuc_0448.
DR   KEGG; amu:Amuc_0448; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_0_0; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   BioCyc; AMUC349741:G1GBX-494-MON; -.
DR   Proteomes; UP000001031; 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..948
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000190203"
FT   MOD_RES         696
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   948 AA;  102650 MW;  E26EDF5979A4EAF0 CRC64;
     MNTHSDFASR HIGPQGEERR EMLDSLGYRT LDELIADIVP ADIRMKAPLD LPAAKSETEA
     LEELRSILRK NKLLKTFIGQ GYYGTITPSV ILRNVLENPG WYTAYTPYQP EIAQGRLEML
     MNFQTMVSSL TGLPVANASL LDEGTAAAEA VTMCRNARPK ANTFFVADTC HPQTISVIRT
     RAAFQGVNII VGDCSSFDPA SIGADLAGVL VQYPDTLGRI CDYTDFFSRV HATGALCVVA
     ADLMALTVIR EPGAFGADIC IGNTQHFGIP MGFGGPHAAY MSCTDALKRR MPGRLIGMSI
     DTLGRPAYRL ALQTREQHIR RDKATSNICT AQVLLAVLAA FYAVYHGQEG LKRIGTEIHL
     KTKSLYKALT EAGIAIENKN FFDTLLLSVP GQADAMVQKA LEAGYNIRRV DADHAAISLD
     ETATCADIAA LASALAGAET SAACDCDAPA WDPVHTRQTP FCTEKAFNSY HSETEMMRYI
     RRLESRDLAL NEAMIPLGSC TMKLNAASEM IPITWPEANS LHPFVPADQS EGIREMLSIL
     SDRLAKITGF AAVSLQPNAG AAGEYAGLLA IRRYQKHAGE GHRNVCLIPT SAHGTNPASS
     AMAGLKVVPV KCDERGNIDM ADLKSQAEAH KDNLSCIMVT YPSTHGVYEQ TIKELCDIVH
     ANGGQVYMDG ANMNAQVGLT CPGCIGADVC HLNLHKTFAM PHGGGGPGIG PIGVAEHLVP
     FLPGHLTLGH EEGAVASAAW GSASIAAICW MYLSMMGPDG LREATEMAIL NANYIAKKLG
     HLFPVLYSGN KGLVAHECIL DPRQLTHDAG LTVDDIAKRL MDYGFHGPTM SFPVPGTLMV
     EPTESEPKKE LDRFIEAMER IHAEITAIIN GTADKEDNVL KNSPHTAEMV SADEWRHPYS
     RSEAAYPVSG LLIHKFWPYV GRVDNVYGDR NLVCTCDTVE EFSKAVEL