ID A0A085Z8K5_9FLAO Unreviewed; 952 AA.
AC A0A085Z8K5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=IX39_09150 {ECO:0000313|EMBL:KFF00769.1};
OS Chryseobacterium formosense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=236814 {ECO:0000313|EMBL:KFF00769.1, ECO:0000313|Proteomes:UP000028713};
RN [1] {ECO:0000313|EMBL:KFF00769.1, ECO:0000313|Proteomes:UP000028713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24722 {ECO:0000313|EMBL:KFF00769.1,
RC ECO:0000313|Proteomes:UP000028713};
RA Pipes S.E., Stropko S.J., Newman J.D.;
RT "Genome of Chryseobacterium formosense LMG 24722.";
RL Submitted (JUL-2014) 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}.
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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC 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}.
CC -!- SIMILARITY: Belongs to the GcvP family.
CC {ECO:0000256|ARBA:ARBA00010756}.
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:KFF00769.1}.
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DR EMBL; JPRP01000001; KFF00769.1; -; Genomic_DNA.
DR RefSeq; WP_034675422.1; NZ_JPRP01000001.1.
DR AlphaFoldDB; A0A085Z8K5; -.
DR STRING; 236814.IX39_09150; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000028713; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 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};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 9..437
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 470..729
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 774..894
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 702
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 952 AA; 105419 MW; B7D7D0C30579F740 CRC64;
MNTEQFVSRH ISLNEADKQA MLEKVGVSNI EELISQTIPS SIRLENDLNI SEALSEYQML
IHSQELAAKN TDYTSYIGFG YHNTLLPSAI QRNIFENPSW YTAYTPYQAE IAQGRLEALL
NYQTVVCDLT GFALANASLL DESTAAAEAM HMFFNNRTKD QKKGGANKFF ISDLVLPQTI
SVLKTKAEGL EIEIVIGDHK THQFDNSYYG VLLQYPGKNG IVLDYTEDIV EYKKLDLQVV
VACDPMALVK LKSPASMGAD CAVGTSQRFG IPLGYGGPHA AFFSCKEDYK RDIPGRIIGV
SQDMYGKRAL RMALQTREQH IKREKATSNI CTAQVLLAVM AGMYAVYHGP KGLNYIADQI
HFKANALKGG LKALGYQTVE EPIFDTVKIL MSEDEKAKLT RMMLDHKLNL NYFTEGVVSI
AINESTTLEK LNVLMASFAQ FKDKQTFKLE IKEGYSIPEE NLRKDEILTE EVFNKYHTET
ELMRYIKRLE RKDLSLTHSM ISLGSCTMKL NAATQMLPLS WAEWGSVHPF VPVNQAGGYQ
QMIHELEKDL AEITGFAGTS LQPNSGAQGE YAGLMVIREY HISRGEGHRN VVLIPQSAHG
TNPASAAMAG MKIVVVKNLE NGEIDFEDLK AKTEQHSENL SCVMITYPST YGFFDANIKE
ITALIHEHGG QVYMDGANMN AQVGYTSPGN IGADVCHLNL HKTFAIPHGG GGPGVGPICV
AKHLVPFLPT NANINVGSKE AIEGISAAPY GSGLILNISY AYIKMLGTAG LKKATEHAIL
NANYLKEILA EHFPILYSNE NGKVAHECIV DFRQFKSLGI EVADVAKRLM DYGFHAPTVS
FPVAGTLMIE PTESESKAEI DRFAEALIAI KHEIDEIANG EADQTNNVLK NAPHTEQIVI
SDSWDKPYSR EKAAYPLDWV RDHKFFASVS RVDEAYGDRN LVCTCEPIEA YM
//
