ID A0A1H2C7M3_9SPHI Unreviewed; 969 AA.
AC A0A1H2C7M3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05216490_4704 {ECO:0000313|EMBL:SDT66433.1};
OS Mucilaginibacter mallensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=652787 {ECO:0000313|EMBL:SDT66433.1, ECO:0000313|Proteomes:UP000199679};
RN [1] {ECO:0000313|EMBL:SDT66433.1, ECO:0000313|Proteomes:UP000199679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP1X4 {ECO:0000313|EMBL:SDT66433.1,
RC ECO:0000313|Proteomes:UP000199679};
RA de Groot N.N.;
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; LT629740; SDT66433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2C7M3; -.
DR STRING; 652787.SAMN05216490_4704; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000199679; 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; 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:UP000199679}.
FT DOMAIN 14..436
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 443..737
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 778..898
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 706
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 969 AA; 106458 MW; B8C27885662B9058 CRC64;
MKLNIDYQEK FQSRHIAPNQ ADTAQMLKTI GVNSLDELID QTVPAGIRLK APLNLPVAKS
EFDYLNTLKQ TASKNKVFKS YIGQGYYDVI VPGVIQRNIL ENPGWYTQYT PYQAEIAQGR
LQALLNFQTM VIDLTGMEIA NASLLDEGTA AAEAMFMQYS LRKNQNANTF FVSQELFPQT
IDILKTRSQP YGIELQIGDH RTAELTDNMF GAIVQYPAGD GEVYNYADYA AQAHAKGIKL
TVVADLMSLV LLTPPGEWGA DIVVGTSQRF GVPMGFGGPH AAFFATKEEY KRSIPGRIIG
VTIDSAGDYA LRMALQTREQ HIRRDKATSN ICTAQALLAI MAGMYAVYHG PQGLKLIAER
IHGLSVLLSD SLTQLGYEQL NDTYFDTVKF DLGVLAGPIH AEALNNEMNF HYKGSVATIS
VDETTSVEDI KTMVRFFAKV KGKTLNDVSF DDLKANVNSI IPAELQRTSA YLAHKLFNSH
HSEHEMLRYI KSLEAKDLSL CHSMIALGSC TMKLNATTEM VPVTWAEFSK MHPFAPVDQT
GGYMQLFDEL NNWLSEITGF AAMSLQPNAG AQGEYAGLMV IRAYHMDRGE GHRNIALIPS
SAHGTNPASA AMAGMKIVVV KCDDNGNIDV ADLKAKAEQY KNDLSCFMVT YPSTHGVFEE
SIIEICEIIH QNGGQVYMDG ANMNAQVGLT SPANIGADVC HLNLHKTFCI PHGGGGPGMG
PIGVAKHLVP FLPGHAVVDI DKGKSIHAVS AAPWGSASIL IISHAYIAMM GADGLTNATR
YAILNANYIK ARLHHHYPVL YTGVHGRCAH EMILDCRSFK PFGIEVTDIA KRLMDYGFHA
PTVSFPVAGT VMVEPTESEP KHELDRFCDA MIAIRHEIDA VEKGLSDKID NPLKNAPHTA
AVITANEWEH PYTRQKAAYP LPYVAAYKFW PSVGRVNDTY GDRTLICSCP PLTDYEFEES
EVTTPEYGT
//
