ID F9RGI2_VIBSN Unreviewed; 1008 AA.
AC F9RGI2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=VIBRN418_17063 {ECO:0000313|EMBL:EGU30765.1};
OS Vibrio sp. (strain N418).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU30765.1, ECO:0000313|Proteomes:UP000003627};
RN [1] {ECO:0000313|EMBL:EGU30765.1, ECO:0000313|Proteomes:UP000003627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N418 {ECO:0000313|EMBL:EGU30765.1,
RC ECO:0000313|Proteomes:UP000003627};
RA Strain E.A., Brown E., Allard M.W.;
RL Submitted (AUG-2011) 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:EGU30765.1}.
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DR EMBL; AFWD01000084; EGU30765.1; -; Genomic_DNA.
DR RefSeq; WP_009387579.1; NZ_AFWD01000084.1.
DR AlphaFoldDB; F9RGI2; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR Proteomes; UP000003627; 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; 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 InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 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; 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..276
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 1008 AA; 111922 MW; 898FB15A893523CF CRC64;
MLPRLHSQPD VDHVVLSFLE ELKAAGFTGD IETQYASRLA VATDNSVYQL LPQAIVHPKS
TEDVALIGQI SIKPVYERVK FSPRGGGTGT NGQSLTQGVV VDLSRHMNKV LEINEQEGWV
RVQTGVVKDQ LNDAVRPFGY FFSPDLSTSN RATLGGMINT DASGQGSLKY GKTSDHVLSL
QAVFADGSIL ESDLSNGLPN QHTYAAHALQ VTEQVCRDKR ADIVAKFPPL NRFLTGYDLK
NAIDESSNQF DLTRVLCGAE GSLAFITEAK LNLTKIPKAR ILVNVKYNSF DSALRNAPFM
VDAQALSVET VDSKVLNLAK EDIVWHTVSD LITDVPDKEM LGINMVEFAG QDITEVEGQL
SALTARLDEM LVNEEAGIIG YQVVNDVASI GKIYNMRKKA VGLLGAAKGR AKPVAFAEDT
CVPPENLADF IDEFRQLLDE KQLNYGMFGH VDAGVLHVRP ALDMCDPLQE KLMHEISDQV
VKLVAKYGGL MWGEHGKGFR SEYGPEFFGE ALFTELRRVK SAFDPHNKMN PGKICTPLES
HEQLVKVSDT KRGFYDRQID VKVRDSFKQA MECNGNGLCF NYDTASPMCP SMKVTADRRH
SPKGRAGLVR EWLRQLTEQG IDILDLEKQS LESASVKTLL DRVRNSFNKR HQYDFSHEVY
EAMNGCLACK ACASQCPIKV DVPSFRSRFL NIYYSRYQRP AKDYLVANIE TMLPLMAKAP
KLVNGVLKQK WVQSLTASTV GYVDAPLLSI PTLAKRVTQL KAFDIQALAA MSSEDKANHV
LIVQDPFTSY YDADVVDDFV QLVIKLGKTP VLLPFKPNGK AQHIKGFLAQ FARNAKSTAM
FLEQVADLSI PMVGVDPALV LCYRDEYNEI LGDKRGEFDV LTVHEWMLPR LSEFDTGSGD
AQPWHLLAHC TEKTKLPNAE KEWGAIFNHF GAKLNTVPVG CCGMAGTFGH EVDKLEMSKD
IFALSWKPRL EALPADRCLV TGYSCRSQVK RFEHVKTKHP LQALLEIV
//
