ID B7IDN5_THEAB Unreviewed; 387 AA.
AC B7IDN5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN OrderedLocusNames=THA_1674 {ECO:0000313|EMBL:ACJ76112.1};
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=484019 {ECO:0000313|EMBL:ACJ76112.1, ECO:0000313|Proteomes:UP000002453};
RN [1] {ECO:0000313|EMBL:ACJ76112.1, ECO:0000313|Proteomes:UP000002453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B {ECO:0000313|EMBL:ACJ76112.1,
RC ECO:0000313|Proteomes:UP000002453};
RX PubMed=19124572; DOI=10.1128/JB.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911,
CC ChEBI:CHEBI:326268; EC=4.1.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00034037};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50};
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00034115}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|ARBA:ARBA00008872, ECO:0000256|RuleBase:RU003737}.
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DR EMBL; CP001185; ACJ76112.1; -; Genomic_DNA.
DR RefSeq; WP_004102495.1; NC_011653.1.
DR AlphaFoldDB; B7IDN5; -.
DR STRING; 484019.THA_1674; -.
DR KEGG; taf:THA_1674; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_026444_1_3_0; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000002453; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR CDD; cd00622; PLPDE_III_ODC; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR002433; Orn_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR11482; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1.
DR PANTHER; PTHR11482:SF6; ORNITHINE DECARBOXYLASE 1-RELATED; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01179; ODADCRBXLASE.
DR PRINTS; PR01182; ORNDCRBXLASE.
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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 29..262
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 263..353
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 325
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 50
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 387 AA; 43384 MW; 06434071BDDC4927 CRC64;
MDKKILNKKL KALAEKHGTP ILVMDLEVVR DNYKRLVENV KNSKIYYAVK ANSHIEILKL
LRDLGSYFDV ASRPEIEKLL SIGVEPERMS FGNTIKKSSD IAFAYEKGIK MFAVDSEMEI
EKIAKNAPGS DIYVRISTNG MEDDADWPLT KKFGTSVDHA ISLVKYAYSL GLNPIGVSFH
VGSQNYNPEN WRVAIREVSV VFEEARRMGI EMKMVNTGGG MPVKYSKNIP TVEEISAVIN
EAIADYIGED VTVILEPGRS MVGNAGTMIT SVILRSQKGE EKWIYTDAGV FHGLTETIQN
IRYEVEVIGK EDEEKEKFVL AGPTCDSVDV MYYDINLPKT TTMDDLVVLY NTGAYTTEYG
TNFNGIPSPK IIFESSIFVK QELFEEV
//
