ID A0A136LP72_9BACT Unreviewed; 833 AA.
AC A0A136LP72;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=UZ12_BCD005002542 {ECO:0000313|EMBL:KXK23464.1};
OS Bacteroidetes bacterium OLB12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1619897 {ECO:0000313|EMBL:KXK23464.1, ECO:0000313|Proteomes:UP000070129};
RN [1] {ECO:0000313|EMBL:KXK23464.1, ECO:0000313|Proteomes:UP000070129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB12 {ECO:0000313|EMBL:KXK23464.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK23464.1}.
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DR EMBL; LNFR01000087; KXK23464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136LP72; -.
DR STRING; 1619897.UZ12_BCD005002542; -.
DR PATRIC; fig|1619897.3.peg.2777; -.
DR Proteomes; UP000070129; 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; 1.
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 1..320
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 351..611
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 651..771
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 579
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 833 AA; 90713 MW; 638CBC40CC652F7F CRC64;
MEALINYQTM VIDLTGMQIA NASLLDEATA AAEAMHLLYA SRKANKKNAN TLFVDENTFP
QVIDLLKTRS EPIGVKLQVG NLDKLDITNL DLFAVYLQNP DNNGAVKDYT TFIESAHEKE
VFVVMGVDLM SLVQIKSPGE MGADVVVGNS QRFGVPMGFG GPHAAFFATK DEFKRQIPGR
IIGVSIDASG NPGYRMALQT REQHIRREKA TSNICTAQVL LSVMASMYAV YHGPEGLKKI
AGRIHGLAQL LENSLAKLGV KQVNAHYFDT LKLAVADKNS IKQKAEAAGI NFRYFNDNHI
GISIDETTSV ADINTILSVF GSATADGKPE TVKLPGSLIR TSPFLTHPVF STHHSEHEML
RYIKKLENKD LSMVHSMISL GSCTMKLNAT TEMIPVTWPE LGQIHPFAPA DQTQGYLEMI
TNLENWLKEI TGFTGVSLQP NSGAQGEYAG LMTIRAYHES RNDGHRTVSL IPASAHGTNP
ASAVMAGMEV VVVKSDAEGK IDVADLKAKA AQYKDKLSCL MVTYPSTHGV FEESIIEICE
TIHANGGLVY MDGANMNAQV GLTSPANIGA DVCHLNLHKT FCIPHGGGGP GMGPICVNDK
LKPFLPGHAV VKTGGDKAIN AISAAPYGSA SILIISYAYI AMMGGEGLTN ATKMAIFNAN
YIKERLAQHF KILYTGANGR CAHEMIVDCR DFKKAGIEVE DIAKRLMDYG FHAPTVSFPV
AGTLMIEPTE SEPKAEMDRF IEALIEIRNE IREVEEGKAD KENNVLKHAP HTAAVITADE
WTRPYSRQKA AYPLAFVKDA KFWPSVSRVD NAYGDRNLVC SCLPLDEYEK AEA
//
