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Database: UniProt
Entry: F8NBS1_9BACT
LinkDB: F8NBS1_9BACT
Original site: F8NBS1_9BACT 
ID   F8NBS1_9BACT            Unreviewed;       630 AA.
AC   F8NBS1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=Premu_0465 {ECO:0000313|EMBL:EGN55947.1};
OS   Hallella multisaccharivorax DSM 17128.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hallella.
OX   NCBI_TaxID=688246 {ECO:0000313|EMBL:EGN55947.1, ECO:0000313|Proteomes:UP000002772};
RN   [1] {ECO:0000313|Proteomes:UP000002772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17128 {ECO:0000313|Proteomes:UP000002772};
RX   PubMed=22180809; DOI=10.4056/sigs.2164949;
RA   Pati A., Gronow S., Lu M., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Mavromatis K., Mikhailova N., Huntemann M., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Detter J.C., Brambilla E.M., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Ivanova N.;
RT   "Non-contiguous finished genome sequence of the opportunistic oral pathogen
RT   Prevotella multisaccharivorax type strain (PPPA20).";
RL   Stand. Genomic Sci. 5:41-49(2011).
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}.
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DR   EMBL; GL945017; EGN55947.1; -; Genomic_DNA.
DR   RefSeq; WP_007572801.1; NZ_GL945017.1.
DR   AlphaFoldDB; F8NBS1; -.
DR   STRING; 688246.Premu_0465; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_10; -.
DR   OrthoDB; 9802658at2; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000002772; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000002772};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW   Rule:MF_01417}.
FT   DOMAIN          80..342
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          369..448
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;  71445 MW;  F4FE482B60C6CA45 CRC64;
     MKKWTIEDSE ELYNIKGWGT SYFGINEQGH VYVSPVKSDV KIDLREVMDE LELRDVTPPV
     LLRFPDILDN RIEKMASCYD KARKEYDFKG HSFIIYPIKV NQMQPVVDEI TTHGRKFNLG
     LEAGSKPELH AVIAQQCKSD SLIICNGYKD ESYIELAILA QKLGKHIFIV VEKLNEIDVI
     AKTAKRLKVM PNIGIRIKLA SSGSGKWAES GGDASKFGLT PSELLEALNK LDEYELHDGV
     KLIHFHIGSQ ITKIRRMQNA LTEAAQYYAN LRKMGYNIEY VDCGGGLGVD YDGTRSSNSE
     SSVNYSIQEY INDCIYAFVD IANKNDIPHP NIITESGRSL AAHHSVLILD VLGVASLPEM
     PEEFEAKPTD HQLVRDLYDI WCNISPKSML EDWHDADQIR EDCLDMFAHG MVDLKTRAEV
     EAMYWSVCHE IDSMAKRMKH VPDELRGLDT LLADKYFCNF SLFQSLPDCW GIDQLFPIMP
     IERLNEAPTR NCTLQDITCD SDGKVANFAV RGSQSNVLPV HALCKNEPYY IGVFLVGAYQ
     EILGDMHNLF GDTTAAHISV KDSTYHIDQI IDGETVEEVL EYVQYNPKKL VRQLEQWVTK
     SVKEGKLPLE EGKEFLATYR SGLYGYTYLE
//
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