ID A0A1W2GYI4_9BACT Unreviewed; 963 AA.
AC A0A1W2GYI4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN00777080_0298 {ECO:0000313|EMBL:SMD41767.1};
OS Aquiflexum balticum DSM 16537.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Aquiflexum.
OX NCBI_TaxID=758820 {ECO:0000313|EMBL:SMD41767.1, ECO:0000313|Proteomes:UP000192333};
RN [1] {ECO:0000313|EMBL:SMD41767.1, ECO:0000313|Proteomes:UP000192333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16537 {ECO:0000313|EMBL:SMD41767.1,
RC ECO:0000313|Proteomes:UP000192333};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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:ARBA00033655, 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}.
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DR EMBL; LT838813; SMD41767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2GYI4; -.
DR STRING; 758820.SAMN00777080_0298; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000192333; Chromosome i.
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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000192333}.
FT DOMAIN 13..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 478..737
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 781..901
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 709
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 963 AA; 105853 MW; 00EEA8AB1A7EEF60 CRC64;
MKIKLDPSTK FEQRHNGPSP KEVQLMLQSI GAASLDELID QTIPKAIQLV KPLDLPKSKT
EASFLRDFKK LALKNKIFKS FIGLGYYDTI VPGVILRNIL ENPGWYTAYT PYQAEIAQGR
LEALINYQTM VMDLTGMEMA NASLLDEATA AAEAMTMLYA SKPREKKNAN KFFVDEKIFP
QTKDLLITRA EPIGIELVIA PLSSLDLTEA NLFGMLLQYP NLDGAVIDHS QLVAAAKENN
VLTAFATDLL SLTLLTPPGE IGADVVVGTS QRFGVPMGYG GPHAAFFATK EAYKRQVPGR
IIGVSVDRDG NKAYRMALQT REQHIKREKA TSNICTAQVL LAVMAGMFAV YHGPKSLKEI
AARTHGLAQL TAKALALLGY KQLNENFFDT IKIKTDAVQQ SKIKAFALSS EMNFRYEEGA
VVLAFDQAKT ISDVKAVVEV FSKSINNKVQ FDWNTMIAEL ELNYPTGLSR TSEYLTHPVF
NLYHSEHEML RYIKRLENKD LSLVHSMISL GSCTMKLNAT AEMVPVTWPE FGQLHPFCPQ
DQAAGYYELF QNLRNWLSEI TGFSDTSLQP NSGAQGEYAG LMVIRAYHMS RGDHHRNIAL
IPTSAHGTNP ASAVMAGMKV VLVKCDESGN IDVEDLKSKA EAHKDELASL MVTYPSTHGV
FEEAIQEICQ IIHDNGGQVY MDGANMNAQV GLTSPGRIGA DVCHLNLHKT FCIPHGGGGP
GMGPICVAEH LVPFLPGNPL IETGGTSAIT AISAAPYGSA SILPISYAYI AMMGGDGLTN
ATKIAILNAN YIKSRLEKHY PILYTGKGGR AAHEMILDCR AFKEVGVEVE DIAKRLMDYG
FHAPTVSFPV AGTLMIEPTE SETMAELDRF CDAMIGIREE IQEVYDGKAD KENNVLKNAP
HTAVLALSDN WDFPYSREKA VYPLPFVKGN KFWPSVRRVD SAYGDRNLVC SCIPVEEYAE
TEV
//