ID Q1Z5X9_9GAMM Unreviewed; 483 AA.
AC Q1Z5X9;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Hypothetical amino acid decarboxylase {ECO:0000313|EMBL:EAS44065.1};
GN ORFNames=P3TCK_12791 {ECO:0000313|EMBL:EAS44065.1};
OS Photobacterium profundum 3TCK.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS44065.1, ECO:0000313|Proteomes:UP000003789};
RN [1] {ECO:0000313|EMBL:EAS44065.1, ECO:0000313|Proteomes:UP000003789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3TCK {ECO:0000313|EMBL:EAS44065.1,
RC ECO:0000313|Proteomes:UP000003789};
RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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:EAS44065.1}.
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DR EMBL; AAPH01000007; EAS44065.1; -; Genomic_DNA.
DR RefSeq; WP_006230580.1; NZ_CH724134.1.
DR AlphaFoldDB; Q1Z5X9; -.
DR HOGENOM; CLU_011856_0_4_6; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000003789; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 483 AA; 52227 MW; 549B9196BC933ACC CRC64;
MSHKFNQYRQ LLNSSLDHAV DYLESLPERP IDKQSSSGSL REAIGGTLPI TGTAPDQVIQ
KLVTDVEEGL IGSGGPRYFG YAIGGSFPVA LAADWLVSAW DQNVPYYVSS PATSIVEETA
AEWMLDLLNL PKTAGVGFTS GAQEAIYTAL ITARNSLLEK AGWDVAANGL YGAPRIHVVM
SDQIHSTIKR ALSMIGIGLK DIKTIPTDQN LRIIPDTLPA ILAECDGPTL VCAQAGCIDS
GAFDPFDEIA SSVEAHPNAW LHIDGAIGLW SAASNTQKHL LKGIEKADSW DTDGHKWFNM
PYDSGMVIVK DAGLLAKAMG GSNMGDYLTD AIAKPDRNAI NFGISASRRA RGVPVYATIK
SLGKEGIQVH LDNCCTLAKR MADKLRNVDG ITILNDVVSN RFSAQFGKGD DAFRDQLTAR
IVHQLQQDGF CYPSTSGYKG LKTMLFSVLS CHTTAQDIDA SAEKIIEIYH MELEKVQQKE
HAV
//
