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Database: UniProt
Entry: A0A0F4QXU5_9GAMM
LinkDB: A0A0F4QXU5_9GAMM
Original site: A0A0F4QXU5_9GAMM 
ID   A0A0F4QXU5_9GAMM        Unreviewed;       958 AA.
AC   A0A0F4QXU5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=TW85_15520 {ECO:0000313|EMBL:KJZ12506.1};
OS   Marinomonas sp. S3726.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ12506.1, ECO:0000313|Proteomes:UP000033747};
RN   [1] {ECO:0000313|EMBL:KJZ12506.1, ECO:0000313|Proteomes:UP000033747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3726 {ECO:0000313|EMBL:KJZ12506.1,
RC   ECO:0000313|Proteomes:UP000033747};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KJZ12506.1}.
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DR   EMBL; JXYC01000018; KJZ12506.1; -; Genomic_DNA.
DR   RefSeq; WP_046018032.1; NZ_JXYC01000018.1.
DR   AlphaFoldDB; A0A0F4QXU5; -.
DR   PATRIC; fig|579484.3.peg.3169; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000033747; 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:UP000033747}.
FT   DOMAIN          17..437
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          619..735
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          778..899
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         701
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT                   ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   958 AA;  104681 MW;  BC01452111598EED CRC64;
     MTSCIRDLLG NDEFIARHIG PDKVEQENML NTIGVDSLEH LIEKTIPQAI RLSNLDMSQQ
     PVSEANALNE LKAIASKNKI ARSFIGMGYH DTFVPAPILR NLLENPGWYT AYTPYQPEIS
     QGRLEALLNF QQMIIDLTGM EISNASLLDE ATAAAEAMTL MLRSNRKKSN LLFVADNLLP
     QTIDVIKTRA DLLEIDFVVD APENVSNHDI FGAIFQYPGK DGEVSDISTL IKACHEQKAL
     VSVAVDLLSL VLLKSPGELG ADIVIGCAQR FGVPMGFGGP HAAYLATKDK FKRSMPGRVI
     GVSIDSHGNK ALRMAMQTRE QHIRREKATS NICTAQALLA MMASFYAVYH GPVGLRQIAT
     RVASLTHSFA KTLNQNGFTT NSSHFDTLVV ETGSKTDAIF LAAQNKLINL WRASDSSLSL
     SVNETTSLTD LVDLAECFGV ELTEDSLADS STDLGIDEGM LRTDAILSHP VFNSHHSETE
     LMRYMHQLEV KDIALNQSMI PLGSCTMKLN ATSEMLPVTW AEFGRIHPFA PQTQVTGYNQ
     LLDELIAMLS KATGYDTVSL QPNSGAQGEY AGLIAIEKYH KSLGEGHRNI CLIPSSAHGT
     NPASAALAGM KVVIVKCDDE GNIDLEDLAA KAELHKDNLS CIMATYPSTH GVFEEHIREV
     CDTVHKFGGQ VYIDGANLNA VLGIAPPGQF GGDVSHLNLH KTFCIPHGGG GPGMGPIGVK
     SHLAPFLPGH SVSPVAGANS NTDQQNGAVS AAPYGSASIL VITWMYIKMM GDRGLKDATF
     NAILNANYIA KRLEDHYPIL FTGVNDTVAH ECIIDIRPLK EESGISEEDI AKRLMDFGFH
     APTMSFPVAG TLMIEPTESE NQEEIDRFCD SMIQIRNEMK KVQAGEWPLE DNPLVNAPHT
     ADALLGEEWQ HAYSRKEAAY PLPWIKDRKY WPPVGRVDNV YGDRNLICEC PPIDSYED
//
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