ID C5BNG1_TERTT Unreviewed; 1024 AA.
AC C5BNG1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=FAD linked oxidase, C-domain protein {ECO:0000313|EMBL:ACR11949.1};
GN OrderedLocusNames=TERTU_2954 {ECO:0000313|EMBL:ACR11949.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR11949.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR11949.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP001614; ACR11949.1; -; Genomic_DNA.
DR RefSeq; WP_015818061.1; NC_012997.1.
DR AlphaFoldDB; C5BNG1; -.
DR STRING; 377629.TERTU_2954; -.
DR KEGG; ttu:TERTU_2954; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_010756_1_0_6; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000009080; 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: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; 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:UP000009080}.
FT DOMAIN 48..280
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 667..699
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1024 AA; 113645 MW; 1DDF22CC21FBF505 CRC64;
MIPKLAPFHD LEQLYVTFLQ ELAQRGFKGE IKSDFSNRVA LSTDNSIYQV LPQGVVYPTS
KDDLVTLAKL AGEDTFKDVV ITPRGGGTGT NGQSLTDGVV VDISRHMNKV LEINAEERWV
RVQTGVVKDQ LNAALKPFNL FFAPDLSTSN RATIGGMINT DASGQGSCVY GKTRDHVLEL
ETVLTDGTIL STRALEPEER SAVLAGDSRS DQLHALVDDI FVSNQALIDE VFPPLNRCMT
GYDLAHIHDQ EGRLNLNNVL CGSEGTLGLI AEAKLNVLPI PRLSALVLVK YADFNSSLRD
ATELMRANPT SVETIDSKVL GLAMQDFIWH QVEEFFVGEN TDAVRGINLV EFTAEDETSL
QQKIDGLTAL LETGIAHQGN TTDFNADTFT PSGRLGYSIA LGRDAVNRIW AMRKRAVGLL
GNAPGEARPI PFVEDTAVPP ENLADFILEF REILDSYQLQ YGMFGHVDAG VLHVRPALDM
KDPKQEDIAW EISDRIADLC HQYGGLLWGE HGKGVRSEYA PKFFGALYPQ LQKIKAAFDP
HNQLNPGKIA TPSAEIELLK IDGVPTRGQH DRQVSQAAWN SFSDAVYCNG NGACYNWNPA
DAMCPSYKGT RDRIHSPKGR ASLVRSWLKM LSDQEVDPDQ ALKSSSILQT PGKFLRSLNK
KRNDDFSHQV YDAMAGCLSC KACASQCPIK VDVPEFRAKF IALYHTRYLR PLKDYLVGTL
EFVLPWCAKV PALYNGVMSA RLVKTVLEKW VGFVDGPLLS KNRLHNIPIA SARRINKLSA
EQRQKTVVIV QDAFTSYFEA PLVQDLAELI RTMGFTPLLA PYKANGKPLH VHGFLKGFQR
VAQRNTRMLH SIAQAGLPLV GVDPSMTHTY RMEYKKFLPE GTEAPQVQLI QEWLADNIEA
LKHVQFRGGQ RFTLLPHCIE QSHATKARDL WADIFTAAGQ QLDTQSLGCC GMSGTYGHEA
RNRDTSRKIY QLSWHNSVEA HEADELLATG YSCRSQVKRE AQKHIRHPLQ ALLSLAAHNF
DSSR
//
