ID A0A136MVT0_9BACT Unreviewed; 956 AA.
AC A0A136MVT0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711};
GN ORFNames=UZ09_BCD002001748 {ECO:0000313|EMBL:KXK37993.1};
OS Bacteroidetes bacterium OLB9.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK37993.1, ECO:0000313|Proteomes:UP000070267};
RN [1] {ECO:0000313|EMBL:KXK37993.1, ECO:0000313|Proteomes:UP000070267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB9 {ECO:0000313|EMBL:KXK37993.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK37993.1}.
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DR EMBL; LNBW01000055; KXK37993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MVT0; -.
DR STRING; 1617420.UZ09_BCD002001748; -.
DR PATRIC; fig|1617420.3.peg.1856; -.
DR Proteomes; UP000070267; Unassembled WGS sequence.
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:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 11..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 475..735
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 775..895
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 703
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 956 AA; 104973 MW; BC73040BDC0F8914 CRC64;
MSSQYLNGFA ERHIGINDAE LSEMLKIIGV DSLDTLINQT VPNGIRMHEN LQLPEALSEY
EYLNMLKKIA SKNKVFKSYI GQGYYDTIVP SVILRNIFEN PGWYTQYTPY QAEISQGRLE
ALLNFQTMVS ELTGLPVANA SLLDEGTAAA EAMAMVEGIH NKKRKNEPAR KFFVDRNIFK
QTLEVAITRA APLHIEIVVG DWKDFDYSDD YFGVMVQYPD ATGEVHDYKA FAAACNEKNI
QVVVIADIMS LVLLEAPGNW GADVVVGNTQ RFGVPMGFGG PHAAYFATRE EHKRVIPGRI
IGVSVDTHGH QALRMALQTR EQHIKREKAT SNICTAQALL AIMAGMYAVY HGPEGLKAIA
SDIYSRTVSL AEQLIAAGYH VINHHYFDTI TIQTDAVNVE AIRNEALANG LNFFYGDNHT
IVISTDEATN WENISEIVDV FSKVSGRKVA SSEKYTTFNS PMKRSEPALS HPVFSAYHTE
SKMMRYIKHL ENKDLSLVHS MISLGSCTMK LNAATEMIPV SWPEFSAIHP FAPAEQTHGY
QQIITELEQY LSEITGFEAC SLQPNSGAQG EYSGLLTIRA YHADKNETHR NVALIPSSAH
GTNPASAVLC GMEVVVVACD ERGNVDVADL KAKAEQYKDN LSCLMITYPS THGVFETSIK
EICTIIHDNG GLVYMDGANM NAQVGLTSPG IIGADVCHLN LHKTFAIPHG GGGPGMGPIC
ANSKLAPFLP GHIMVKTGGS KAIQAVSSAP FGSASVLLIS YGYIRMLGSK GLTDATKYAI
LNANYLKARL EKAYDILYSG ENGRAAHEMI VDLRPFKAIG ISAEDVAKRL MDYGFHAPTL
SFPVAGTLMI EPTESEDKAE LDRFCDAMLE IRKEIDQVAS GEMDEKSNVL TNAPHTSEVV
TSDEWSYTYP RTKAAYPLSY IAARGKFWPS VGRVDSAYGD RNLVCTCPPM ESYMSE
//
