ID A0A1I0NUC4_9BACT Unreviewed; 967 AA.
AC A0A1I0NUC4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05216290_1474 {ECO:0000313|EMBL:SEW05223.1};
OS Roseivirga pacifica.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=1267423 {ECO:0000313|EMBL:SEW05223.1, ECO:0000313|Proteomes:UP000199437};
RN [1] {ECO:0000313|Proteomes:UP000199437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12402 {ECO:0000313|Proteomes:UP000199437};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOIR01000001; SEW05223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0NUC4; -.
DR STRING; 1267423.SAMN05216290_1474; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000199437; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199437}.
FT DOMAIN 14..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 466..740
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 783..903
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 711
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 967 AA; 106285 MW; 765534335AACDE58 CRC64;
MTKIDLRKTQ KFEDRHNGPD AKEVQEMLEV IGAPSLDALI EETVPAGIRM KEPLNLPLPK
SEFQFLKDLR HIAAQNKMFK SYIGMGYYDT IVPGVIQRNI LENPGWYTAY TPYQAEIAQG
RLEALVNFQT MVMDLTGMEI ANASLLDEAT AAAEAMFMFA GQRKKDKKSA NTFFVDENTF
PQTIEVLKTR SIPVGIDLEI GAVADLDLTR EDLYGILIQY PAGDGKVINY SSLIASAHEN
NVFVTAAADL MSLALLTPPG EMGADAVVGT TQRFGVPMGY GGPHAAYFAT KEAFKRQIPG
RIIGASIDSQ GNQAYRMALQ TREQHIRREK ATSNICTAQV LLGVMAGMYG VYHGSQGIKH
IAFKIHGFAQ LVNKGLKHLG FNQLNDLYFD TLRIETDLAM AEKVKTIAEV NQVNFRYFED
GSIGIAVDET TRVEDVQVIF EIFAEATGQV MDFDLDGEAA DLEVALPADL ERKSDFMTHP
VFNQYHSEHE MLRYIKKLEN KDLSLVHSMI SLGSCTMKLN ATAEMVPVTW PEFGGIHPFA
PTYQTRGYHM MFHDLVDWLS EITGFYDVSL QPNSGAQGEY AGLMVIRAYH ESRGEGHRNI
AIIPSSAHGT NPASAVMAGM KVVIVNCDEK GNIDVEDLKA KVEQHSNELS CLMVTYPSTH
GVFEESIKDM CALIHEHGGQ VYMDGANMNA QVGLTSPGII GADVCHLNLH KTFCIPHGGG
GPGMGPIGVA EHLAPFLPGN PVIESGGDSA ITAVSAAPWG SASILTISYA YIAMMGAEGL
TNATKMAILN ANYIKAKLEK EFKILYAGSK GRCAHEMIVD CRDFKNQKVE VEDIAKRLMD
YGFHAPTVSF PVAGTVMIEP TESESKSELD RFCEAMLSIR QEIREIADGI AEEGSNVLKN
APHTAAMVLE GQWEMPYSRE KAVYPAPYVK EAKFWPTVAR IDSAYGDRNL MCSCIPVSDY
QEEEAMA
//
