ID   A0A1V3NIV1_9GAMM        Unreviewed;      1288 AA.
AC   A0A1V3NIV1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:OOG24808.1};
GN   ORFNames=B1C78_08280 {ECO:0000313|EMBL:OOG24808.1};
OS   Thioalkalivibrio denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=108003 {ECO:0000313|EMBL:OOG24808.1, ECO:0000313|Proteomes:UP000189462};
RN   [1] {ECO:0000313|EMBL:OOG24808.1, ECO:0000313|Proteomes:UP000189462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALJD {ECO:0000313|EMBL:OOG24808.1,
RC   ECO:0000313|Proteomes:UP000189462};
RA   Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T.,
RA   Sorokin D.Y., Muyzer G.;
RT   "Genomic diversity within the haloalkaliphilic genus Thioalkalivibrio.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:OOG24808.1}.
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DR   EMBL; MVBK01000044; OOG24808.1; -; Genomic_DNA.
DR   STRING; 108003.B1C78_08280; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000189462; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR021817; DUF3400.
DR   InterPro; IPR022153; DUF3683.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF11880; DUF3400; 1.
DR   Pfam; PF12447; DUF3683; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 2.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189462}.
FT   DOMAIN          169..403
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          810..841
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1288 AA;  143860 MW;  97243120B1F6E45E CRC64;
     MPDTAPVPVQ ATQRIREIPY NYTSFSDREI VIRFLGEEMW HALNELRGER RTGVSARMLF
     EVLGDMWVVT RNPYIQDDLL DNRRRLTALI EAMDHRLDQI VARADGNERA LELAGRAREA
     VRRFEDWFPE QRALRKRTLR RLSKHTRRDN IHFDGFARVS HVTDATDWRV ELPFVVVTPD
     SEAEMAGVVA ACIELGLTVI PRGGGTGYTG AAVPLDERSA VINTEKLEGL GSVEMRRIPG
     VEESVPTVRA EAGVVTRRVS ERAAEEGLVF AVDPTSQDAS TIGGNIAMNA GGKKAVLWGT
     TIDNLASWRM VTPDAKWLEV ERVGHNLGKI HDQETVRFRI TRYSADGVTP EGAPEEISAP
     GQSFRKLGLG KDVTDKHLGG LPGVQKEGCD GLITSAVFVL HRMPKHIRTV CLEFYGDDLH
     EAVPAIVEIK DRLDGDPQVR LSGLEHLDER YVRAVRYTPK GARGERPKMV LLADVCSDDE
     DAVGRAASAM VRLANARNGE GFVAVSAEAR KRFWSERART AAIAAHTNAF KINEDVVIPL
     DRLAEYSEGI ERINIVQSIT NKLRMVAEML ECLKGDHPEL RELLAIENDE GRRWFEGKRR
     AATQHLEGVQ ARWKLILAHL DEDAVAHDAL LDERSRENLR PGDRLINLLL RRSLRISYRR
     EVSRPLWDIF DGLELEPVRK RLEAIHDRVL TSRLFVALHM HAGDGNVHTN IPVNSNDYAM
     MHEAERIVDQ VMALARRLGG VISGEHGIGI TKMQYLEPAQ VDAFAGYKQR VDPEGRFNRG
     KLMPGSGLAN AYTPSLRLVQ QEALILEQSE LGALNEDIKD CLRCGKCKPV CSTHVPRANL
     LYSPRNKILA SGLILEAFLY EEQTRRGLSL RHFDEMNDVA DHCTICHKCE SPCPVNIDFG
     DVTIRMRNIL KQRGRRRVKP TTLASMAFLN IKDPATIKLM RRVMVQWGYA GQRLGHALFR
     RLGLLNGARP ASTTGRASLP AQVVHFVKKP MPPGLPARTT RAMLGLEDPS QVPVVRDPAR
     ADEPGDAVFY FPGCGSERLF SQVGLATIAM LYDTGAKTVL PPGYLCCGYP QTSAGDVDKG
     RAITTENRVL FHRVANTLNY LDIRTVIVSC GTCMDQLLKY EFGQIFPGCR LLDIHEYLME
     KGLSLKGVPG VQYLYHDPCH TPMKTHAPVQ VASRLMGQEV RLSDRCCGEA GTFAVSRPDI
     ATQVRFRKEE ELRAGIRGFT GRDEAVDGDV KMLTSCPACQ QGLARYREDT GLDTDYIVVE
     MANRLLGEGW QERFIERARS GGIERVLL
//