ID   A0A2M6UZG1_9BURK        Unreviewed;      1029 AA.
AC   A0A2M6UZG1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:PIT71603.1};
GN   ORFNames=B9Z41_16735 {ECO:0000313|EMBL:PIT71603.1};
OS   Limnohabitans sp. JirII-31.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1977908 {ECO:0000313|EMBL:PIT71603.1, ECO:0000313|Proteomes:UP000228925};
RN   [1] {ECO:0000313|EMBL:PIT71603.1, ECO:0000313|Proteomes:UP000228925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JirII-31 {ECO:0000313|EMBL:PIT71603.1,
RC   ECO:0000313|Proteomes:UP000228925};
RA   Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA   Simek K., Ghai R.;
RT   "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL   Submitted (APR-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:PIT71603.1}.
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; NESA01000020; PIT71603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M6UZG1; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000228925; 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   CDD; cd03128; GAT_1; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02754; CCG; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
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; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
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:UP000228925}.
FT   DOMAIN          60..288
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          659..688
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1029 AA;  112325 MW;  9A8BE7679BE58A27 CRC64;
     MNAPLPRHIT ETASQVFERV ASTSNEVAGR LAARLRTETE GQVLFSAADR GRYATDASIY
     QVTPVGVFVP RHAHEVPIAM AICRDLGVPI VPRGGGTSQC GQTTGAGLVI DHSKHIRQIV
     HLDVEQRTVE VEPGLVLDHL NAELKAHGLW FPVDVSTSAQ ASLGGMAGNN SCGSRSIAYG
     NMVHNVVGAS AWLGDGDLLQ WGRYDASSGR ARQIGDFVKR LANELQPDIE AHWPKVLRRV
     AGYNLDIFCN QNERPYTDDG SVNLAHLLVG SEGTLAMTKS LTLRLSELPR AKVLGVVNFP
     SFYKAMDAAQ HIVKLGDGTL TAVELVDRTM IDLSLQNPAF APTIRTALIG EPEAVLLVEF
     AGADKESLKP KMRQLVELMG DLGLPGSVVE MIDDAPQKNL WEVRKAGLNI MMSLKGDGKP
     VSFIEDCAVP LESLAEYTDA LTEVFKKHGT KGTWYAHASV GTLHVRPILD MRRDGATKMR
     AIAEEASALV RQYKGAYSGE HGDGLCRGEW VAWQFGPKIT EALRQIKQTL DPLHLLSPQR
     VVNPPKMDDT RLMRYGQPNG MPYQVIPIQT ALDWSAWNVH NDPATEQTTA PGTGGDPALG
     FAKAVEMCNN NGTCRKFDAG TMCPSYRVTR DEQHLTRGRA NTLRLALSGQ LGTDALTSEE
     LLQTMDLCVG CKGCKRDCPT GVDMARMKIE TLHQYKRYHG HTLKDRLIGF LPRYAKHAAR
     WSGLLNLRNR VPLLAKLAQS LTGLSAERSW PTWQRDHFFN RSTLGSTAEE VLIAPKPVVL
     FVDTFNGYFE SDNARAAMRV LQAAGYQVHV ASKTRQGHGS DQGHLCCGRT FLANGMVDQA
     REHAQELLNA LLPFAKRGIP IVGLEPSCLL TLRDEALVLG LGEVAHKVSE QAMLFEEFLA
     REAQAGRLDA LKSKLEPTRQ PILLHGHCHQ KAFGLMPPVL EVIRLIPGAK PQLIESSCCG
     MAGSFGYEAS HLEVSKAMAE LSLLPAVRAE PDALVVADGT SCRHQIADGA QRQAVHVAKL
     LSDHLKHHA
//