ID F4G8P7_ALIDK Unreviewed; 1305 AA.
AC F4G8P7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:AEB83324.1};
GN OrderedLocusNames=Alide2_0913 {ECO:0000313|EMBL:AEB83324.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB83324.1, ECO:0000313|Proteomes:UP000007938};
RN [1] {ECO:0000313|EMBL:AEB83324.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RX PubMed=21742888; DOI=10.1128/JB.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
RN [2] {ECO:0000313|EMBL:AEB83324.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP002657; AEB83324.1; -; Genomic_DNA.
DR RefSeq; WP_013721498.1; NC_015422.1.
DR STRING; 596154.Alide2_0913; -.
DR KEGG; adk:Alide2_0913; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_262983_0_0_4; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000007938; Chromosome.
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:InterPro.
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; 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; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007938}.
FT DOMAIN 180..413
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 828..857
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1305 AA; 144791 MW; 5835B0AD472E2FF7 CRC64;
MNAPIALAAL QAQGSEPVRL REIPYNYTSF SDREIVIRLL GAQAWDVLDH LRRERRTGRS
ARMLYEVLGD IWAVQRNPYL QDDLIHNPQR RKMLVDAMRH RMGEIEKRRT PQEDPERDRR
VAQLVEAANR AIAEFDATLV EVAGMRKLVA RRLARHTAKD NIKFDGLSRV SHVTDATDWR
VEFPFVVLTP DTEGETAALV KECIELDLTI IPRGGGTGYT GGAIPLSWRS AVINTEKLEA
MTEVEMVRLP GLAHDVPTVW TEAGVVTQRV ADAAERGGYV FAVDPTSIEA SCIGGNIAMN
AGGKKAVLWG TALDNLASWR MVTPQAQWLE VTRINHNLGK IHDAEVASFE LAYFEADGRT
PVRTERLDIP GKSFRKEGLG KDVTDKFLSG LPGVQKEGTD GLITSARWIV HRMPAHTRTV
CLEFFGSAKE AVPSIVEIKD FMFAEQKRSG VLLAGLEHLD DRYLKAVGYA TKSKKGGGRL
PKMVLIGDLV GDDADAVARA TAEVVRIANS RSGEGFTAVS SEARKQFWLD RKRTAAISRH
TNAFKINEDV VIPLPRMAEY TDGIERINIE LSLRNKLKLC DALQDFFARP DLPCAKQGDA
LPDAELLGDR VAQAQALVAE VRALWQGWLD DVARLFPQLQ DHSLRASWKT QLRQPLAEIF
VGAAFEPLMQ EAAAIHKQVL KGRVWVALHM HAGDGNVHTN IPVNSDDYEM LQTAHEAVGR
IMQLARSLDG VISGEHGIGI TKLEFLSDEE LAPFADYKRR IDPQGHFNRG KLLRNQELQG
QVYQALEANS AHNGPRRSLP FADLTNAYTP SFGLMGYESL IMQQSDIGQI VASVKDCLRC
GKCKPVCSTH VPRANLLYSP RNKILATSLL AEAFLYEEQT RRGISSHHWQ EFEDVADHCT
ICHRCYNPCP VKIDFGDVTM AMRSLLVKMN KKSWRPGNKL AMAMLNATDP RTINLLRAGM
VNVGFKAQRL AVDALRSVSK AQTARPPATV GTAPIKEQVI HFVNKKLPGG LPTRTARALL
DIENKDYVPI IRDPQTSADS EAVFYFPGCG SERLFSQVGL ATQAMLWHAG VQTVLPPGYL
CCGYPQRGNG LQDKAEKMIT DNRVLFHRVA NTLNYLDIKT VVVSCGTCYD QLQGYEFDKI
FPGSRIIDIH EYLLEKGITL PAGQGYLYHE PCHNPMKLGD SMKTVRALVG DKVLKSDRCC
GESGTLGVSR PDVSTQVRFR KTEEIRKGEA QLRGSGAVGA TDNIKILTSC PSCLQGISRY
QDDLQTGLLE ADYIVIEMAR QILGENWLPE YVQRANAGGI ERVLV
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