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Database: UniProt
Entry: H0TRN4_9BRAD
LinkDB: H0TRN4_9BRAD
Original site: H0TRN4_9BRAD 
ID   H0TRN4_9BRAD            Unreviewed;       957 AA.
AC   H0TRN4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 62.
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   ECO:0000313|EMBL:CCE09122.1};
GN   ORFNames=BRAS3843_3040007 {ECO:0000313|EMBL:CCE09122.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE09122.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
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:ARBA00033655, 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:CCE09122.1}.
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DR   EMBL; CAFK01000229; CCE09122.1; -; Genomic_DNA.
DR   RefSeq; WP_008971633.1; NZ_CAFK01000229.1.
DR   AlphaFoldDB; H0TRN4; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000002686; 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:UP000002686}.
FT   DOMAIN          17..440
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          444..730
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          774..895
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|HAMAP-Rule:MF_00711,
FT                   ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   957 AA;  102687 MW;  F0653AECD0075744 CRC64;
     MNAPFKPLDD AATTFARRHI GPSPRDVAAM LETIGAKSLS ELMAQTLPAS IRQAAPLDIG
     PSLSETEALS HMRGLAAQNQ VFTSLIGQGY SGTIMPAVIQ RNILENPAWY TAYTPYQPEI
     SQGRLEALFN FQTMICDLTG LDVANASLLD EATAAAEAMA LAERSASAKA KAFFVDKNIH
     PQTLAVLKTR AEPLGWRLIV GDPATDLDGS DVFGGILQYP DTTGRLRDPR ADIAKLRAKG
     ALAILAADLL ALTLIASPGE LGADIAIGSA QRFGVPMGYG GPHAAYMAVR DTLKRSLPGR
     IVGLSVDSRG APAYRLALQT REQHIRREKA TSNICTAQVL LAVIAAMYAV YHGPEGLAAI
     ARNVHRRAAV LAAGLRKLGF APDSDAFFDT VSVDAGAKRD DIVARALNEK INLGLGDRAL
     RVALDETTTP EIVEAVWRAF GGELSYASIE AEAREALPAG LKRQSRFLTH PVFHAHRSET
     EMLRYLRKLA DRDLALDRAM IPLGSCTMKL NATTEMIPLT WPEFASLHPI APRAQAAGYH
     ALFGRLEDWL CRISGYDAVS LQPNSGAQGE YAGLLAIRGY HAARGESHRK VCLIPSSAHG
     TNPASAHMAG MEVVVVACDA GGNVDVVDLK AKAEKHTANL AAIMITYPST HGVFEEHIGE
     ICDIVHAHGG QVYLDGANLN AQVGLARPGD YGADVSHFNL HKTFCIPHGG GGPGMGPIGV
     KAHLAPFLPG HPATDGAIVR PVGPVSAAPY GSASILTISY IYMLLMGGEG LQRATEIAIL
     NANYIAARLD AHFPVLYRNE RGRVAHECIV DPRPLKQTSG VTVDDIAKRL IDYGFHAPTM
     SFPVPGTLMI EPTESESKAE LDRFCDAMIA IRNEIAEVEQ GRFKIEASPL RHAPHTVHDV
     ADDDWNRAYR RSEGCFPAGS SRTDKYWCPV GRVDNVYGDR NLVCSCPPLA DYAEAAE
//
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