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Database: UniProt
Entry: K2KNH5_9PROT
LinkDB: K2KNH5_9PROT
Original site: K2KNH5_9PROT 
ID   K2KNH5_9PROT            Unreviewed;      1031 AA.
AC   K2KNH5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=TH2_15627 {ECO:0000313|EMBL:EKF07334.1};
OS   Thalassospira profundimaris WP0211.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Thalassospira.
OX   NCBI_TaxID=1177928 {ECO:0000313|EMBL:EKF07334.1, ECO:0000313|Proteomes:UP000007365};
RN   [1] {ECO:0000313|EMBL:EKF07334.1, ECO:0000313|Proteomes:UP000007365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP0211 {ECO:0000313|EMBL:EKF07334.1,
RC   ECO:0000313|Proteomes:UP000007365};
RX   PubMed=23209215; DOI=10.1128/JB.01903-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of Thalassospira profundimaris Type Strain WP0211.";
RL   J. Bacteriol. 194:6956-6956(2012).
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:EKF07334.1}.
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DR   EMBL; AMRN01000008; EKF07334.1; -; Genomic_DNA.
DR   RefSeq; WP_008891425.1; NZ_AMRN01000008.1.
DR   AlphaFoldDB; K2KNH5; -.
DR   PATRIC; fig|1177928.3.peg.3208; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   Proteomes; UP000007365; 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   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 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; IPR009051; Helical_ferredxn.
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          74..306
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1031 AA;  114292 MW;  3D75D3DE1FA62D2A CRC64;
     MSVPAPAATP VTNPVTNASN KSVIKKLPAL TPDRSLDSLT LGFLKTLEAE GKFAGEIHAD
     FPTRLINATD NSVYQVMPTA VLQPKTRGDI NVVMELAGRE KFSEVKITPR GGGTGTNGQS
     LNNTIILDTS KHLNNILGFD AERGLVHVEP GVVLDQLNAW LKPHGYFFPP AVSTASRATV
     GGMIGSDSSG KGSRIYGKTS HYIHDMTTVL IDGTDFNTRA MNATEAKDTM DRADRVGQLY
     KKVHDEIAPR RDQIKSTFPE MNRGLTGYNL KEAVSDTGDM NLSFLIAGAE GSLGMVKEIT
     FRVIPMPKFK AVTVVRYDSF DSALRHVKTL VQFDPVAIES IDDKVMKLAE QDESWHMLGK
     LLGTENSTTP TRGFNVVEFV GETEAEVAAK QTELKSYLEA NPTEDFSPIG FVQATDPAQI
     AAIWSIRAKS VGLLGNLEGK RRATPFVEDT AVPPENLADF IAEFRALLDA EGLDYGMFGH
     VDVGCLHVRP LLDMMDEEDE ARIRRVSDAV AALTKRYNGL IWGEHGKGFR GEYSPVYFGP
     ELYDVLRRIK EAFDPEGQLN PGKIASPYSK NTPITAIDEA PMRGQFDRQI EDALRDEYLN
     ATRCNGNGAC FNWDLMDAMC PSYKVTRSRV HSPKGRAGMI REWIRQLSVG TDPMNKDLAV
     INGRDFSHDV YEAMAGCLSC KACAGQCPVK VDIPEMKSRF LETYHTRYKR PIKDHVIASL
     ESMAPLLAKA PGLFNALQSI PPTPWIFKRF IGLTDLPKLH GQSLKSGLRA RGIGKFRQAE
     LDSLSGDEKA KSVILVQDCF TTHYDTHVVL AHVDLLQRLG YRVFVPPYRP NGKAMHVKGF
     LKRFDYQAKQ NDIVLGKIAK SGVPMIGIEA SVTLTYRQEY EQRLSNRPDY RVHLFHEWLA
     GEIEHGRLTP PKIDNGVNMS APDAPARLFP HCTEKTSIPD VGVKWQKIFD AFGLKLTTEK
     TGCCGMAGVY GHETRHQETS RELYELSWKK KVDATGPQNM LVTGYSCRCQ VDRYEGVKPQ
     HPVEYLAKLI A
//
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