ID A0A1M5P0T2_STRHI Unreviewed; 398 AA.
AC A0A1M5P0T2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN ORFNames=SAMN05444320_11730 {ECO:0000313|EMBL:SHG95381.1};
OS Streptoalloteichus hindustanus.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Streptoalloteichus.
OX NCBI_TaxID=2017 {ECO:0000313|EMBL:SHG95381.1, ECO:0000313|Proteomes:UP000184501};
RN [1] {ECO:0000313|EMBL:SHG95381.1, ECO:0000313|Proteomes:UP000184501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44523 {ECO:0000313|EMBL:SHG95381.1,
RC ECO:0000313|Proteomes:UP000184501};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FQVN01000017; SHG95381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5P0T2; -.
DR STRING; 2017.SAMN05444320_11730; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000184501; Unassembled WGS sequence.
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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184501}.
FT DOMAIN 26..269
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 335
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 49
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 398 AA; 42319 MW; C098D3938B28162B CRC64;
MSMRLGSRLR AALAAAEEDQ IVLDLAGIEH QYEALARELP GARVRFAMKA CPVDDVLACL
AGRGAGFDAA SPGEISQALG AGASVHDIHY GNTVKSDQNI VDAYRLGVRD FATDSVEDVM
AIAAHAPGSR VFCRLATTGA GAVWGLSRKC GCSGEDAVRV LDTARLLGLT PSGLSVHVGS
QQMTADAWQD AVDRLTEALV ALRDRGIQVD HVNLGGGLPA LGYLDRSGRP LDPPLDEIFA
TIRAGVARLR QVAGADLDIV LEPGRHLVAD HGAIRAHVVR MTARRQLSGD REHWLYLSCG
KFNGLYEVDQ VQYRLLFPGH HDEEHVPAVV AGPTCDSDDT FGAARFPVPV PRSVASGDPV
WIVSCGAYST SYTTVGFNGF SPLPLNLLPG EHRAKAHA
//
