PDAD1_ARCFU
ID PDAD1_ARCFU Reviewed; 157 AA.
AC O27983;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase 1;
DE Short=PvlArgDC 1;
DE EC=4.1.1.19;
DE Contains:
DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase 1 subunit beta;
DE Contains:
DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase 1 subunit alpha;
GN Name=pdaD1; OrderedLocusNames=AF_2301;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58145; EC=4.1.1.19;
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000250};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PdaD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88952.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000782; AAB88952.1; ALT_INIT; Genomic_DNA.
DR PIR; E69537; E69537.
DR AlphaFoldDB; O27983; -.
DR SMR; O27983; -.
DR STRING; 224325.AF_2301; -.
DR EnsemblBacteria; AAB88952; AAB88952; AF_2301.
DR KEGG; afu:AF_2301; -.
DR eggNOG; arCOG04490; Archaea.
DR HOGENOM; CLU_114389_0_0_2; -.
DR OMA; VFCVMSR; -.
DR PhylomeDB; O27983; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR Gene3D; 3.50.20.10; -; 1.
DR HAMAP; MF_01404; PvlArgDC; 1.
DR InterPro; IPR016104; Pyr-dep_his/arg-deCO2ase.
DR InterPro; IPR016105; Pyr-dep_his/arg-deCO2ase_sand.
DR InterPro; IPR002724; Pyruvoyl-dep_arg_deCO2ase.
DR PANTHER; PTHR40438; PTHR40438; 1.
DR Pfam; PF01862; PvlArgDC; 1.
DR PIRSF; PIRSF005216; Pyruvoyl-dep_arg_deCO2ase; 1.
DR SFLD; SFLDG01170; Pyruvoyl-dependent_arginine_de; 1.
DR SUPFAM; SSF56271; SSF56271; 1.
DR TIGRFAMs; TIGR00286; TIGR00286; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyruvate; Reference proteome.
FT CHAIN 1..40
FT /note="Pyruvoyl-dependent arginine decarboxylase 1 subunit
FT beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023304"
FT CHAIN 41..157
FT /note="Pyruvoyl-dependent arginine decarboxylase 1 subunit
FT alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023305"
FT SITE 40..41
FT /note="Cleavage (non-hydrolytic)"
FT /evidence="ECO:0000250"
FT MOD_RES 41
FT /note="Pyruvic acid (Ser)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 157 AA; 17205 MW; 2A77CE5332244078 CRC64;
MLPRKVFFTK GVGRHTDPLV SFELALRDAG IEKFNLVTVS SIYPPYCEIV EAEKGLSELF
PGQIVFCVMS RMTSNEQGKR IFASVGAAIP PDPSLNGYLT EYHGYCNGED AGRHAEESAA
YMLKTAFEIE PARTFNITVE ADVEDCTTVV AAAVFVI