ID R1IPL6_9GAMM Unreviewed; 450 AA.
AC R1IPL6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Orn/DAP/Arg decarboxylase 2 {ECO:0000313|EMBL:EOD79392.1};
GN ORFNames=D515_01845 {ECO:0000313|EMBL:EOD79392.1};
OS Grimontia indica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1056512 {ECO:0000313|EMBL:EOD79392.1, ECO:0000313|Proteomes:UP000011223};
RN [1] {ECO:0000313|EMBL:EOD79392.1, ECO:0000313|Proteomes:UP000011223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK16 {ECO:0000313|EMBL:EOD79392.1,
RC ECO:0000313|Proteomes:UP000011223};
RX PubMed=24465608;
RA Singh A., Vaidya B., Khatri I., Srinivas T.N., Subramanian S., Korpole S.,
RA Pinnaka A.K.;
RT "Grimontia indica AK16(T), sp. nov., Isolated from a Seawater Sample
RT Reports the Presence of Pathogenic Genes Similar to Vibrio Genus.";
RL PLoS ONE 9:E85590-E85590(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50};
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|RuleBase:RU003737}.
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:EOD79392.1}.
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DR EMBL; ANFM02000021; EOD79392.1; -; Genomic_DNA.
DR AlphaFoldDB; R1IPL6; -.
DR eggNOG; COG0019; Bacteria.
DR Proteomes; UP000011223; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
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; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43727:SF2; DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 65..282
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 317..413
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 385
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 76
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 450 AA; 49926 MW; 556F4189DF0F341D CRC64;
MDTMTVVEAN NGFDTRFPAK EDLSLPYRQL FPLITKAANT PFHAMLPHRI KQNIVGLKHV
LSRYLGERFQ VLYAMKTNRS AALVKAAAEE GIGIDVSSLE EFQLALTQGV CGRDCSLSGP
FKSVEFLTLA LRQNARIVVD SDEELLQIQN LAVSIGKTAR VLLRWNAEQP HTRFGMNTVK
LKAASLVADS LSNIELEGAG FHLSGYCPLE RGKALSDLLD AADALRYGAD IRWKVINIGG
GYPLRYVEEA TWRRFQNAID RQDFVAGRMP KSFYPYWHPD TLETAVEKVL IESGNAERLK
ANNIELSVEP GRALTDGAGF TAFEVLGTKT TNAGDHCVVV KGLSFSFSET WFNSEFIVDP
VHLPASQETT KSTNPVRAYI AGQSCLEEDV LTYRKVPFSQ MPKAGDLLVF NNTAGYLMDL
LETRFHGLPI PNKVVLDNKE DSFSIEEVRG
//
