ID K7AF84_9ALTE Unreviewed; 279 AA.
AC K7AF84;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Isopenicillin-N synthase {ECO:0000313|EMBL:GAC33970.1};
DE EC=1.21.3.1 {ECO:0000313|EMBL:GAC33970.1};
GN ORFNames=GPLA_3079 {ECO:0000313|EMBL:GAC33970.1};
OS Paraglaciecola polaris LMG 21857.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129793 {ECO:0000313|EMBL:GAC33970.1, ECO:0000313|Proteomes:UP000006322};
RN [1] {ECO:0000313|EMBL:GAC33970.1, ECO:0000313|Proteomes:UP000006322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21857 {ECO:0000313|EMBL:GAC33970.1,
RC ECO:0000313|Proteomes:UP000006322};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
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:GAC33970.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAER01000083; GAC33970.1; -; Genomic_DNA.
DR RefSeq; WP_007105736.1; NZ_BAER01000083.1.
DR AlphaFoldDB; K7AF84; -.
DR STRING; 1129793.GPLA_3079; -.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000006322; Unassembled WGS sequence.
DR GO; GO:0016216; F:isopenicillin-N synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682,
KW ECO:0000313|EMBL:GAC33970.1}.
FT DOMAIN 145..253
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 279 AA; 31335 MW; 7FD33502E4306972 CRC64;
MQLLAVDYLA PDADKKFVES LRQTGFGVLK NHPIEQSTVT SIYQNWQAFF NRDDKLHYAF
DNQSHDGFFS TKVSETAKGF KKKDIKEYFH YYPWGKCPPD LKQELQDYYQ AANNLASELL
AWVEKYSPSE VAALYSEPLS GMAKDSDQTL LRVLHYPPIT GAEEPDAIRA AAHEDINLLT
ILPSANEPGL QVKGTGDEWI DVPCDFGTLI VNIGDMLQEA SGGYFPSTSH RVINPKGADQ
SKSRISLPLF LHPRPEVVLS ERHTAKSYLA ERLRELGVA
//