ID Q1Q0T2_KUEST Unreviewed; 809 AA. AC Q1Q0T2; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 05-JUL-2017, entry version 30. DE SubName: Full=Hypothetical (Di heme) protein {ECO:0000313|EMBL:CAJ73613.1}; GN ORFNames=kuste2861 {ECO:0000313|EMBL:CAJ73613.1}; OS Kuenenia stuttgartiensis. OC Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Kuenenia. OX NCBI_TaxID=174633 {ECO:0000313|EMBL:CAJ73613.1}; RN [1] {ECO:0000313|EMBL:CAJ73613.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16598256; DOI=10.1038/nature04647; RA Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., RA Taylor M.W., Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., RA Fonknechten N., Vallenet D., Segurens B., Schenowitz-Truong C., RA Medigue C., Collingro A., Snel B., Dutilh B.E., OpDenCamp H.J.M., RA vanDerDrift C., Cirpus I., vanDePas-Schoonen K.T., Harhangi H.R., RA vanNiftrik L., Schmid M., Keltjens J., vanDeVossenberg J., Kartal B., RA Meier H., Frishman D., Huynen M.A., Mewes H., Weissenbach J., RA Jetten M.S.M., Wagner M., LePaslier D.; RT "Deciphering the evolution and metabolism of an anammox bacterium from RT a community genome."; RL Nature 440:790-794(2006). RN [2] {ECO:0000313|EMBL:CAJ73613.1} RP NUCLEOTIDE SEQUENCE. RA Galiano M.C., Trento A., Ver L., Carballal G., Videla C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000213|PDB:5C2V, ECO:0000213|PDB:5C2W} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 28-809 IN COMPLEX WITH RP CALCIUM AND HEME. RX PubMed=26479033; DOI=10.1038/nature15517; RA Dietl A., Ferousi C., Maalcke W.J., Menzel A., de Vries S., RA Keltjens J.T., Jetten M.S., Kartal B., Barends T.R.; RT "The inner workings of the hydrazine synthase multiprotein complex."; RL Nature 527:394-397(2015). 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; CT573071; CAJ73613.1; -; Genomic_DNA. DR PDB; 5C2V; X-ray; 2.70 A; A/D=28-809. DR PDB; 5C2W; X-ray; 3.20 A; A/D=28-809. DR SMR; Q1Q0T2; -. DR DIP; DIP-61794N; -. DR KEGG; ag:CAJ73613; -. DR KO; K20934; -. DR BioCyc; MetaCyc:MONOMER-15348; -. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR Gene3D; 1.10.760.10; -; 1. DR InterPro; IPR009056; Cyt_c-like_dom. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:5C2V, ECO:0000213|PDB:5C2W}; KW Calcium {ECO:0000213|PDB:5C2V, ECO:0000213|PDB:5C2W}; KW Heme {ECO:0000213|PDB:5C2V, ECO:0000213|PDB:5C2W}; KW Iron {ECO:0000213|PDB:5C2V, ECO:0000213|PDB:5C2W}; KW Metal-binding {ECO:0000213|PDB:5C2V, ECO:0000213|PDB:5C2W}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 809 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004195495. FT METAL 385 385 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:5C2V, ECO:0000213|PDB: FT 5C2W}. FT METAL 403 403 Calcium 1. {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. FT METAL 404 404 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:5C2V, ECO:0000213|PDB: FT 5C2W}. FT METAL 407 407 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:5C2V, ECO:0000213|PDB: FT 5C2W}. FT METAL 409 409 Calcium 1. {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. FT METAL 591 591 Iron (heme 1 axial ligand). FT {ECO:0000213|PDB:5C2V, ECO:0000213|PDB: FT 5C2W}. FT METAL 689 689 Iron (heme 2 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. FT METAL 772 772 Iron (heme 2 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. FT METAL 795 795 Calcium 2. {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. FT METAL 797 797 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:5C2V, ECO:0000213|PDB: FT 5C2W}. FT METAL 799 799 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:5C2V, ECO:0000213|PDB: FT 5C2W}. FT METAL 801 801 Calcium 2. {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. FT BINDING 583 583 Heme 1 (covalent). {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. FT BINDING 586 586 Heme 1 (covalent). {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. FT BINDING 685 685 Heme 2 (covalent). {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. FT BINDING 688 688 Heme 2 (covalent). {ECO:0000213|PDB:5C2V, FT ECO:0000213|PDB:5C2W}. SQ SEQUENCE 809 AA; 90244 MW; 4D60D075EB87A7CF CRC64; MGKRKLGVIA SAFVAGALVC GSTLVNAEPV MTGGPVQGKA LWTDYSGMSK EVQGPVSQIL FTQSPRTAKG DPYQNYPHYI PEGSRIVLFD LNTKELKVLT NDFATAFDPC TYWDGKKFAF AGVHKKGGGC QIWEMNIDGS GLRQMTDLKG TCRSPIYYAA GSIEEGEGRI IWRDRYFEGD WKEHGMVEKT GMIIFSGSPE GVMDEFHNPY AYNLYRLDTQ GGKIIQRITG HVLSGIEFPH LNTTIDQITY NLSSNFDPWL TPDGNILFSS VQANGSRAGG EGRVMICVDN WDGAYPRPIY GNCDGEIGGT SGRSQAKITF GDRKIVYVES PYMNWGVGQL AAVSWDAPFN KTYEKLTGKD GGLYRSPYPL PDDRMLVSYA ERGDFGIYWF NFSKCAAGDK VYDDPNWNDH QPAPVYVKYK PRWINTFTAG KNFGVTVVTY QPFDQVKVEG YPHSWGTWIC FDTTLSDQPV GPYPHQKAKN VSHGDIKAVR IIQGYQCVEP DSTRFRVGAG AHLLGGERSS SNSGTAFQQR GIIGYQYVES DGSTVTSQLS DVPYYMQILD DKGMSVQTAL TWAYLRPYHG RICSGCHYGS YRGRAFKNIH AKALYNWWYD DRSHYDSPFA FRYLKFDNDG NYKGVKHGED VVVPSDIYYG GPSGTTSQPV EGLTLDKQRT VDFRRDIQPI LDAKCAMCHD SNNPPNLGGG LELVSVDGIA AYSRAYNSLL EPQRGKDPNI GGKYVNPSAA INSLLVWRLY EAELSANAPR EKIFPIEGRL LHNKFLTQDE RYAIVEWIDL GAQWDNIPGP DFYPGYLVK //