ID A0A1V6LNK2_9FLAO Unreviewed; 946 AA.
AC A0A1V6LNK2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BUL40_15220 {ECO:0000313|EMBL:OQD41556.1};
OS Croceivirga radicis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceivirga.
OX NCBI_TaxID=1929488 {ECO:0000313|EMBL:OQD41556.1, ECO:0000313|Proteomes:UP000191680};
RN [1] {ECO:0000313|EMBL:OQD41556.1, ECO:0000313|Proteomes:UP000191680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSG9 {ECO:0000313|EMBL:OQD41556.1,
RC ECO:0000313|Proteomes:UP000191680};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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}.
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:OQD41556.1}.
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DR EMBL; MTBC01000013; OQD41556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6LNK2; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000191680; 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:UP000191680}.
FT DOMAIN 9..436
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 450..725
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 769..886
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 697
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 946 AA; 104182 MW; 963CE2F1B90004CF CRC64;
MNTELFASRH IGVREEDLSK MLETVGVKDL EELMYQTIPD DIRLKKELEL PKAMSEHEFL
GHVQKLSEKN KIFKTYIGLG YHNTLTPSVI KRNILENPGW YTAYTPYQAE IAQGRLEALL
NFQTMVTDLT GMEIANASLL DESTAAAEAM TMLYDLRSRQ QKKDGVLKFF VDENVLPQTL
SLLETRATPL EIELVIGNPE QFTYTTDFFG SLLQYPGKHG QVKDFKEFTQ QATANEIKVA
VAADLLSLVL LKAPGEWGVD VVVGTTQRFG IPLGYGGPHA AFFATKEAYK RNIPGRIIGL
TKDTDGNPAL RMALQTREQH IKRDKATSNI CTAQVLLAVM AGMYAVYHGP KGLQYIANSI
HEKTKQLTGM LAEVGFAQTN TVFFDTIQVK VADAEALKEV ALNNEINLNY VDSNTVTISL
NEATSFEDVK DILAVFSEVG NTSDTGTSFE EIPDSLKRDT EFLTHEVFNS YHSETDLMRY
IKKLERKDLA LNHSMISLGS CTMKLNAASE MLPLSWANWG NLHPFVPINQ AEGYQVMLKS
LEDYLTEITG FAATSLQPNS GAQGEFAGLM TIRAYHEANG QGHRNICIIP ASAHGTNPAS
AVMAGMKVVV TKTDENGNID LVDLEEKVKL HSENLSSLMV TYPSTHGVFE SSIKQITQLI
HDHGGQVYMD GANMNAQVGL TNPATIGADV CHLNLHKTFA IPHGGGGPGV GPICVAEQLK
PFLPSNPVVA TGGNNAITAI SAAPWGSALV CLISYGYIRM LGAKGVTNAT KYAILNANYI
KERLAGSYEV LYTGERGRAA HEMIIDCRPF KENGIEVTDI AKRLIDYGFH APTVSFPVAG
TMMIEPTESE SKQELDRFCD AMLSIREEID QANAAEPNNV LKNAPHTMAM VTADQWDFPY
SRKDAAYPLE FVFENKFWPS VRRTDEAFGD RNLICTCAPI EAYAEA
//
