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
//