ID A0A2U1ZUJ3_9MICO Unreviewed; 971 AA.
AC A0A2U1ZUJ3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:PWD50648.1};
GN ORFNames=C8046_08260 {ECO:0000313|EMBL:PWD50648.1};
OS Serinibacter arcticus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Serinibacter.
OX NCBI_TaxID=1655435 {ECO:0000313|EMBL:PWD50648.1, ECO:0000313|Proteomes:UP000245166};
RN [1] {ECO:0000313|EMBL:PWD50648.1, ECO:0000313|Proteomes:UP000245166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCH200 {ECO:0000313|EMBL:PWD50648.1,
RC ECO:0000313|Proteomes:UP000245166};
RA Thakur V., Kumar V., Singh D.;
RT "Genome assembly of novel Miniimonas species PCH200.";
RL Submitted (MAR-2018) 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:PWD50648.1}.
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; PYHR01000002; PWD50648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1ZUJ3; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000245166; 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 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; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 48..264
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 596..627
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 971 AA; 102073 MW; A61A78234AB48A55 CRC64;
MTTLTRPPGA GRPPEDATAA LLSDLARVTE ADAGRRRRAE YSTDASNYRV VPQVVTFPRH
VDEVLATLEV ARTHRAPVTA RGAGTSVAGN AVGPGVVIDF SRHLHAIGEI DPEQRTAVVQ
PGVVMSSLQT AAAPHGLWFG PDPSTKNRAT LGGMIGNNAC GPHALAYGRT ADNVRSLDVV
DGAGRRFTAG SGRDALEAVA GLDRLVAANL ALMRTELGRF TRQVSGYSLE HLLPERGSHL
ARALVGTEGS VVTLLGATVE LHPLPTAPVL VVLGYADMPS AADAVVPLAA LKPLAIEGMD
ARLVDVVRQH VGSVPDLPRG AGWLFCEVGG ADETEALANA AALVAASDCV DSLITTDKAK
SAALWRIRAD GVGLAGRTPA GRQAWPGWED AAVPPENLGA YLRDFDALLA QYGVDGLPYG
HFGDGCIHVR IDLPLDRPGD VPDFEAFMND AARLVGSYGG SLSGEHGDGR ARGGLLHHMY
TPEALGLFEQ FKGLLDPSDH LNPGIVVRPA PVTANLRRPQ AITLGTKGFA LPHDGGDLTQ
AVHRCVGVGK CRADNSSAGG FMCPSYQATG DERNATRGRA RVLQELANGS FVQGWDAPEV
ADSLDLCLSC KACGRDCPAG VDMATYKAEV TYRRYKGKLR PMSHYVLGWL PRWAKLATAF
PPVAGLANLA LRVAPLRKAV FAVSGIDGRR KMTAFTTHRF SRWFPQRSGT ALTARGRTPD
DGASDGVAAT GTRTRDVILW ADSFSEHLDP AGAQAMVRLL EKAGYTVRIP SSDACCGLTW
ISTGQLDGAR KRLARTLDVL GPAAAKGVPI IGVEPSCTAV LRSDLVELLP DDPRSAQVAG
AVRTLAELLT DPELGPGEDW APPSLVGTTV VAQPHCHQHS VMGFDADAML LARTGATVTQ
LAGCCGLAGN FGMEKGHYEV SVAVAENALL PALREAPEGA VYLADGYSCR TQAEQLAGTR
GTTLAQLLLA E
//