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Database: UniProt
Entry: Q2C9F0_9GAMM
LinkDB: Q2C9F0_9GAMM
Original site: Q2C9F0_9GAMM 
ID   Q2C9F0_9GAMM            Unreviewed;       960 AA.
AC   Q2C9F0;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Oxidoreductase, FAD-binding, putative {ECO:0000313|EMBL:EAR57535.1};
GN   ORFNames=SKA34_08113 {ECO:0000313|EMBL:EAR57535.1};
OS   Photobacterium sp. SKA34.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=121723 {ECO:0000313|EMBL:EAR57535.1, ECO:0000313|Proteomes:UP000005284};
RN   [1] {ECO:0000313|EMBL:EAR57535.1, ECO:0000313|Proteomes:UP000005284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKA34 {ECO:0000313|EMBL:EAR57535.1,
RC   ECO:0000313|Proteomes:UP000005284};
RA   Hagstrom A.J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:EAR57535.1}.
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DR   EMBL; AAOU01000001; EAR57535.1; -; Genomic_DNA.
DR   RefSeq; WP_006644553.1; NZ_CH724141.1.
DR   AlphaFoldDB; Q2C9F0; -.
DR   HOGENOM; CLU_013186_0_0_6; -.
DR   OrthoDB; 9789605at2; -.
DR   Proteomes; UP000005284; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          129..208
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          232..400
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   960 AA;  109977 MW;  20BBED3B8507A68A CRC64;
     MSPPQKTQTT LKHAQQADIE TMVNCIYYSS HELMNFIFVD KQTALSVLHK LVVQPQGLFS
     YRFGWLYNHN DITQGAVLGY SRLQLQQQEL TGAIQLLFAS PLHLKWRILT TVRKALANYV
     PLPSKDAFYI NNVAIFSNAR GQGLGTSLLD DLCHQLKQQG YRCIELDVTF CNKGAIRFYQ
     RYGFYQVSQS GSEALSQKYG LPLLLRLRYV LPTSTSSQTT NTNIIKEVSR LYSVGVDDVY
     IPGTIEQLQT MLQSTSKPIS IGGGRYSMGG QTAHPDTLHI DMRGLNRILE LDINKQTIRV
     QAGARWRDIQ AKIKDYGLAV KIMQTYANFT IGGSLSVNCH GRYVSLGPLI LSVNEIKLLL
     DDGTAVIASP TQHSELFYGA IGGYGALGII VEAELSLTND SHIKRLHKKI PLTEYPAFFA
     ENIKGDPDAV FHNADMLPPE FNRVQVITWF STDQAVNVAP RQSRKLYLAE KYMLWTITEA
     PFGNWLREYI YEPVLYWRNK ITTRNDEANY YVAELEPISR TETTYVLQEY FIPVGNIEQF
     TPRMTEILTR YTVNTVNISI RHSHPDPGSI LAWAREEVFA FVLYYKQGAS KAEQEKVAIW
     TRELIEAAIN AGGCYYLPYQ PHARFDQFHR AYPNATKLFE LKAKWDSDYR FRHCLWDKYY
     RQNNDPTLLS PKEINTSEFR QIYNTVKQRD AFYLFLQNIY HLYPEHLFHQ LIMDACQYIN
     TDEAIYHEIQ YSLPDIKPAL ADIRFALPAL AKQKKEMTEQ TQTILPTGRH LNGYLEIGST
     GRYVNGLKKA LKLSGKVFIS NENAPDNSPA EIVERGSIKL VGEFFALDDY EPIPDNIIED
     NSLDLITCYI GLHHCPPEKL DSYIDSIYRV LKPEGYFILR DHDAGTDQQR TFCSLVHTVF
     NAGLHISWQE NQAELRNFQG IDYWISALEK KGLKDSKQYL LQAHDPSLNT LMCFKKVQYP
//
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