ID D0SSK5_ACILW Unreviewed; 399 AA.
AC D0SSK5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Putative 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component {ECO:0000313|EMBL:EEY91202.1};
GN ORFNames=HMPREF0017_00215 {ECO:0000313|EMBL:EEY91202.1};
OS Acinetobacter lwoffii SH145.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY91202.1, ECO:0000313|Proteomes:UP000018425};
RN [1] {ECO:0000313|Proteomes:UP000018425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; GG705055; EEY91202.1; -; Genomic_DNA.
DR AlphaFoldDB; D0SSK5; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_0_6; -.
DR Proteomes; UP000018425; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:EEY91202.1};
KW Oxidoreductase {ECO:0000313|EMBL:EEY91202.1}.
FT DOMAIN 2..292
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 311..398
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 399 AA; 43483 MW; 4CE9A2A75545DC24 CRC64;
MGAGQAGASA ILELRGNKYE GKITLIGDES HLPYERPPLS KDVILKPEDT KIEILSEQKL
ADLGVETIRG NGVMKINAEA KTVELLNGDV VAYDKLLLAT GGAARRLPNF DALGKHVYTL
RNLEDSQALV PVLQAGRRII LIGGGVIGLE LASSARYKDC QVTVIEMGPM VMGRCSPQIL
SEFLLEQHRQ NQVDVRLETK IADCRLDGEE VVVTLEGGEE LRADAVVYGI GIVPNAQLAL
DAGLDVDVAI KVNEHCQTSN ADIYAAGDVA TQLRDCGNHR RVETWENANL QAGIFARHVM
GVEHPKANPA WFWTDQLNIN FQFVGDMAAA EWHIRGEMDA AKGADNSFVM YGVTDGQIVG
GITVNAAKEM RHLKKMISKN TAFDVEKHLD IAQDLRKIA
//
