ID G1VBK1_9BACT Unreviewed; 630 AA.
AC G1VBK1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000256|HAMAP-Rule:MF_01417};
DE Short=ADC {ECO:0000256|HAMAP-Rule:MF_01417};
DE EC=4.1.1.19 {ECO:0000256|HAMAP-Rule:MF_01417};
GN Name=speA {ECO:0000256|HAMAP-Rule:MF_01417};
GN ORFNames=HMPREF0666_00784 {ECO:0000313|EMBL:EGW47999.1};
OS Prevotella sp. C561.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=563031 {ECO:0000313|EMBL:EGW47999.1, ECO:0000313|Proteomes:UP000003086};
RN [1] {ECO:0000313|EMBL:EGW47999.1, ECO:0000313|Proteomes:UP000003086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C561 {ECO:0000313|EMBL:EGW47999.1,
RC ECO:0000313|Proteomes:UP000003086};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella sp. C561.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000256|ARBA:ARBA00002257, ECO:0000256|HAMAP-Rule:MF_01417}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01417};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01417};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01417, ECO:0000256|PIRSR:PIRSR001336-50};
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01417}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357, ECO:0000256|HAMAP-
CC Rule:MF_01417}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01417}.
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:EGW47999.1}.
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DR EMBL; ADCT01000043; EGW47999.1; -; Genomic_DNA.
DR RefSeq; WP_009010970.1; NZ_JH114141.1.
DR AlphaFoldDB; G1VBK1; -.
DR STRING; 563031.HMPREF0666_00784; -.
DR PATRIC; fig|563031.3.peg.772; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_10; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000003086; Unassembled WGS sequence.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06830; PLPDE_III_ADC; 1.
DR Gene3D; 1.10.287.3440; -; 1.
DR Gene3D; 1.20.58.930; -; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_01417; SpeA; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR040634; Arg_decarb_HB.
DR InterPro; IPR041128; Arg_decarbox_C.
DR InterPro; IPR002985; Arg_decrbxlase.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR01273; speA; 1.
DR PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 1.
DR Pfam; PF17810; Arg_decarb_HB; 1.
DR Pfam; PF17944; Arg_decarbox_C; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR PRINTS; PR01180; ARGDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_01417};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01417};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01417};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01417};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW Rule:MF_01417};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01417,
KW ECO:0000256|PIRSR:PIRSR001336-50};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW Rule:MF_01417}.
FT DOMAIN 79..342
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 368..445
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 576..629
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 499
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417,
FT ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 630 AA; 71391 MW; E1C52532DE5C15E1 CRC64;
MKKWTIEDSQ ELYNISGWGT SYFGINDAGD VYVTPCKDNT QIDLRDVMDE LALRDVTPPV
LLRFPDILDN RIEKTSSCFE KARKEYDFKG ENFIIYPIKV NQMQPVVEEI ISHGRKFNLG
LEAGSKPELH AVIAVQCQSD SLIVCNGYKD QSYIELALLA QKMGKRIFIV VEKLNEIELI
ARAAKKLNVK PNLGIRIKLA SSGSGKWADS GGDASKFGLT SSELLQALET LDSKGLHDCL
HLIHFHIGSQ ITKIRRIQTA LNEAAQYYVN LRKMGYNVDF VDCGGGLGVD YDGTRSASSE
SSVNYSIQEY VNDCVYTFVD AANKNNIPHP NIITESGRSL SAHHSVLVID VLETASLPEM
SEDFEAKDTD HQLVKDLYDI WDNLDSRNML EDWHDAEQIR EEALELFSHG LVDLKTRAEI
EAMYWSVCHE INNLAKNMKH VPDELRNMDK LLADKYFCNF SLFQSLPDSW AIDQLFPVMP
IQRLNERPSR NATLQDITCD SDGKISNFVA MGRSSHVLPI HPLKKNESYY LGVFLVGAYQ
EILGDMHNLF GDTNAVHVSV KDGSYHIDQI FDGETVEEVL EYVQYNPKKL VRQLEIWVTK
SVKQGKISLE EGKEFLSNYR SGLYGYTYLE
//
