ID A0A0D6N094_9PROT Unreviewed; 972 AA.
AC A0A0D6N094; A0A6N3SQL2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=Abci_005_011 {ECO:0000313|EMBL:GAN59417.1};
OS Acetobacter cibinongensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=146475 {ECO:0000313|EMBL:GAN59417.1, ECO:0000313|Proteomes:UP000032671};
RN [1] {ECO:0000313|EMBL:GAN59417.1, ECO:0000313|Proteomes:UP000032671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4H-1 {ECO:0000313|EMBL:GAN59417.1,
RC ECO:0000313|Proteomes:UP000032671};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acetobacter cibinongensis 4H-1.";
RL Submitted (NOV-2012) 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:GAN59417.1}.
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DR EMBL; BAMV01000005; GAN59417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6N094; -.
DR STRING; 1231339.Abci_005_011; -.
DR Proteomes; UP000032671; 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 35..458
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 477..752
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 792..913
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 724
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 972 AA; 103606 MW; 35F767A672D120C9 CRC64;
MFTLASGPDR SPASSADSLP AFSGLKTEAG SFVPRHIGPS RQDVATMLEV VGAPTLDALM
EQTLPADIRI AQPMGIGAGW SEGEVLAHLR KLAGQNQVMT SLIGQGYYGT VLPAVIQRNI
LENPAWYTAY TPYQPEISQG RLEALLNFQT MITELTGLDI ANASLLDEAT AAAEAMAMAH
RVAKSKATAF FVDAETHPQT LAVLKTRAEP LGIALVVGAP DTDLHAAEVF GALFQYPGTT
GALKNPRAAI EALHAAGGIA VMAADPLALT LLTSPGELGA DIAIGSTQRF GIPMGFGGPH
AAYMAVRDAW KRNLPGRLVG VSVDSQGRPA YRLALQTREQ HIRREKATSN ICTAQVLLAV
IAGMYAVYHG PEGLKAIARR VHGLTTTLAE GLRALGVAVE TEHFFDTLTV QVGGGAADIL
ARARSAGINL RDVGQGRLGL SLDETTTPDT VLAVWSAFCT EQGRVETMAK ALAPATQAIP
AELVRQSAFL TQSVFSSCQS ETDMLRYLRR LSDKDLALDR TMIPLGSCTM KLNATVEMLP
ITWPGFCDIH PFAPAEQTAG YQALFTDLEK WLCAISGYDA VSFQPNSGAQ GEYAGLLAIS
AYHRARGQAN RTVCLIPASA HGTNPASAQM AGMKVVVVKC DTDGNIDLTD MREKVAAHAA
TLSAVMITYP STHGVFEESM REICDLVHEA GGQVYVDGAN MNAQVGLARP ADYGGDVSHF
NLHKTFCIPH GGGGPGMGPI GVRAHLKDFL PGNPADAGTT LAVSAAPYGS ASILPISWAY
IRLMGDEGLK RATEVAILNA NYIVSRLVDA YPVLYRGGKG RVAHECIIDL RPLKDAFGVT
VDDIAKRLVD YGFHAPTVSF PVAGTFMIEP TESEGKAELD RFCDAMLAIR DEVRAIEAGV
LTAEHSPLRH APHTGAMVTV EPWPHTYTRQ EACFPPGVNP SRKYWPTVSR IDNAHGDRNL
VCSCPDISEW ME
//
